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New Aspects of Meat Quality: From Genes to Ethics

New Aspects of Meat Quality: From Genes to Ethics

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New Aspects of Meat Quality: From Genes to Ethics

Longueur:
1,491 pages
17 heures
Sortie:
Mar 22, 2017
ISBN:
9780081006009
Format:
Livre

Description

New Aspects of Meat Quality: From Genes to Ethics provides a reference source that covers what constitutes meat quality in the minds of consumers, marketers, and producers in the 21st century, using the same scientific authority as texts on traditional meat quality values.

Traditional measures in meat quality, such as texture, waterholding, color, flavor/aroma, safety/microbiology, and processing characteristics are still important, however, additional quality attributes now have huge importance in the purchasing intentions of consumers in many countries. These include, amongst others, animal welfare, the impacts of meat on human health, quality assurance schemes, organic/free range, ethical meat production, and the desirability of genetically modified organisms.

The book is divided into three main sections, with the first section covering the developments in our understanding of how muscle structure affects the eating qualities of cooked meat. The second section highlights recently developed techniques for measuring, predicting, and producing meat quality, and how these new techniques help us minimize variability in eating quality and/or maximize value. The final section identifies the current qualities of consumer and public perceptions, and what is sustainable, ethical, desirable, and healthy in meat production and consumption.

  • Brings together top researchers in the field to provide a comprehensive overview of the new elements of meat quality
  • Provides a reference source that covers the new aspects of meat quality with the same scientific authority as texts on traditional meat quality values<
  • Edited by an extremely well respected expert in the field who is an Associate Editor of the journal Meat Science (published by Elsevier), the largest global journal within this area
Sortie:
Mar 22, 2017
ISBN:
9780081006009
Format:
Livre

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New Aspects of Meat Quality - Elsevier Science

New Aspects of Meat Quality

From Genes to Ethics

Woodhead Publishing Series in Food Science, Technology and Nutrition

Edited by

Peter P. Purslow

National University of Central

Buenos Aires Province, Tandil, Argentina

Table of Contents

Cover

Title page

Copyright

List of Contributors

Acknowledgments

Chapter 1: Introduction

Abstract

1. What is meat quality?

2. The aim and structure of this book

Part I: Developments in Our Understanding the Association Between Muscle Structure and the Basic Eating Qualities of Cooked Meat

Chapter 2: Muscle Structure, Proteins, and Meat Quality

Abstract

1. Introduction

2. Structure and function of muscle

3. Muscle protein changes and meat quality

4. Summary

Chapter 3: Myogenesis and Muscle Growth and Meat Quality

Abstract

1. Introduction

2. Myogenesis

3. Postnatal muscle growth

4. Intrauterine growth restriction and implications for performance and meat quality

5. Muscle protein turnover

6. Mutations in pigs with effect on growth and meat quality

7. Conclusions

Chapter 4: Perimortal Muscle Metabolism and its Effects on Meat Quality

Abstract

1. The conversion of muscle to meat

2. Fresh meat quality

3. Aberrant postmortem metabolism mutations

Chapter 5: What’s New in Meat Oxidation?

Abstract

1. Introduction

2. Oxidation in muscle foods

3. Oxidation and consumer health

4. Advances in antioxidant strategies

5. Conclusions

Chapter 6: Current Developments in Fundamental and Applied Aspects of Meat Color

Abstract

1. Introduction

2. Biochemistry of fresh meat color

3. Practical aspects of fresh meat color

4. Conclusions

Chapter 7: Advances in the Understanding and Measurement of Meat Texture

Abstract

1. Meat texture—underlying structures

2. Major processes affecting final texture

3. Measuring texture of meat

4. Future trends

Chapter 8: Developments in Our Understanding of Water-Holding Capacity in Meat

Abstract

1. The significance of water-holding

2. Hypotheses about mechanisms of water-holding

3. Factors influencing water-holding capacity

4. Future trends in water-holding research

Chapter 9: Current Challenges in Enhancing the Microbiological Safety of Raw Meat

Abstract

1. Introduction

2. Trends in pathogen prevalence associated with different raw meats

3. The one health era

4. Pathogens of concern

5. Intervention strategies to control pathogens of importance to food safety in meat production and processing

6. Interventions at the processing level to enhance microbiological safety of meat

7. The age of Big Data

8. Conclusions and future trends

Chapter 10: Quality Assurance Schemes in Major Beef-Producing Countries

Abstract

1. Carcass grading and classification

2. Quality grading

3. Future and emerging considerations

4. Conclusions

Part II: New Techniques for Measuring, Predicting and Producing Meat Quality, and How They Help us Minimize Variability in Eating Quality and/or Maximize Value

Chapter 11: Transcriptomics of Meat Quality

Abstract

1. Introduction

2. Intramuscular fat

3. Tenderness

4. Drip loss, meat color PSE, and DFD meat

5. Systems biology approaches

6. The intersection of transcriptomics, genotyping, and phenotyping (genetical genomics) in meat quality

7. Conclusions

List of abbreviations (excluding gene and protein names)

Chapter 12: Gene and Protein Expression as a Tool to Explain/Predict Meat (and Fish) Quality

Abstract

1. Introduction

2. New insights in proteomic tools

3. Proteomics to understand meat quality

4. Proteomics in association with other genetic and omic approaches

5. Conclusions

Chapter 13: NMR Spectroscopy and NMR Metabolomics in Relation to Meat Quality

Abstract

1. Introduction

2. NMR spectroscopic studies of perimortal metabolism

3. NMR spectroscopic studies of meat processing

4. NMR metabolomics studies on meat

5. NMR metabolomics studies of non–meat-derived samples emphasizing meat quality

6. Conclusions and future trends

Chapter 14: X-ray Contrast Tomography and Raman Spectroscopy Methods Show Heat-Induced Changes in Meat

Abstract

1. Introduction

2. X-ray phase-contrast tomography

3. Raman spectroscopy

4. Discussion

Chapter 15: Cooking and Novel Postmortem Treatments to Improve Meat Texture

Abstract

1. Introduction

2. Cooking

3. High pressure processing

4. Shockwaves

5. Pulsed electric field

6. Ultrasonics

7. Smartstretch/Smartshape and Pi-Vac

8. Summary and conclusions

9. Future trends

Chapter 16: New Sources of Animal Proteins: Cultured Meat

Abstract

1. Introduction

2. Technology

3. Technical conditions for feasibility

4. Nutritional value

5. Safety

6. Acceptance

7. Disclaimer

Chapter 17: New Sources of Animal Proteins: Edible Insects

Abstract

1. Introduction

2. The role of insects in the diet of people in tropical countries

3. An ecolabel for edible insects?

4. Insects and a welfare label

5. Nutrition

6. Processing

7. Food safety

8. Farming

9. Consumer attitudes

10. Discussion and conclusions

Acknowledgment

Part III: The Current Qualities of Consumer and Public Perceptions; What is Sustainable, Ethical, Desirable and Healthy

Chapter 18: Meat Nutritive Value and Human Health

Abstract

1. Meat and human evolution

2. Nutritive value of meat

3. Concluding remarks

Chapter 19: Meat and Cancer Evidence for and Against

Abstract

1. Introduction

2. Epidemiological and experimental data

3. Potential mechanisms

4. Metabolomics

5. Conclusions

Chapter 20: Manipulating the Fatty Acid Composition of Meat to Improve Nutritional Value and Meat Quality

Abstract

1. Introduction

2. Fatty acid composition of meat

3. Fatty acids and human health

4. Dietary manipulation of meat fatty acid composition and the effects on meat quality

5. Alternative approaches to improving fatty acid composition and preserving quality

6. Future possibilities

Cross-Reference

Acknowledgments

Chapter 21: Fundamentals of Animal Welfare in Meat Animals and Consumer Attitudes to Animal Welfare

Abstract

1. Introduction

2. Priority welfare issues concerning animals produced for meat and eggs

3. Attitudes of consumers toward farm animal welfare in Europe

4. Attitudes of consumers toward animal welfare in North America

5. The consumers’ perception of animal welfare in other world regions

6. Conclusions

Chapter 22: How to Work With Large Meat Buyers to Improve Animal Welfare

Abstract

1. Introduction

2. Development of welfare assessment tools for slaughter plants

3. Economic buying power coupled with numerical scoring brought about great improvements

4. Keep audit programs and guidelines simple and clear

5. Standards should be strict but sensible

6. Transparency needed in animal industry

7. Conclusions

8. Disclaimer

Chapter 23: Veterinary Drug Residues in Meat-Related Edible Tissues

Abstract

1. Introduction

2. Concepts and regulations on drug residues

3. Official drug residue monitoring programs

4. Causes of unsafe drug residual concentrations in meat and edible tissues

5. Factors affecting drug residual levels in meat/edible tissues

6. Economic and public health impact of drug residues in food-producing animal tissues

7. Concluding remarks

Chapter 24: Specific Veterinary Drug Residues of Concern in Meat Production

Abstract

1. Drugs used in mass medication: antibacterial and antiparasitic compounds

2. Growth-promoting agents

3. Concluding remarks

Chapter 25: Ethics of Meat Production and Its Relation to Perceived Meat Quality

Abstract

1. Introduction

2. World population growth and food crisis

3. What are ethics?

4. Quality systems to ensure ethical animal agriculture

5. Animal husbandry and ethics

6. Shifts in animal production and consumer perceptions

7. Carcass and meat quality systems

8. New technologies, meat production, and quality

9. Conclusions

Chapter 26: Ethical and Sustainable Aspects of Meat Production; Consumer Perceptions and System Credibility

Abstract

1. Introduction

2. Ethical and sustainable aspects of meat production

3. Consumer attitudes and behavior in relation to meat

4. Systems to ensure transparency and sustainability in meat production

5. Discussion

Chapter 27: Sensory Perceptions and New Consumer Attitudes to Meat

Abstract

1. Background

2. A brief history of carnivory

3. Changing meat consumption patterns in the 21st century

4. What we love about meat; the unique nutritional and sensory properties of muscle foods

5. Why some consumers don’t like to eat meat: vegetarianism, veganism, conscientious omnivorism, and flexitarianism

6. An innate preference for meat?

7. Gender divide; do men and women have different attitudes to meat?

8. Popular culture and meat in the digital era

9. Comminuted chicken nuggets, beef burgers and sausages—is this the inevitable future of meat consumption?

10. Meat substitutes

11. Changes in flavor/texture/color with extreme aging

12. The meat fat paradox

13. Sustainably grass fed meat—arguably the most natural food in the modern diet?

14. Organic versus nonorganic

15. Conclusions

Index

Related Titles

Improving Food Quality through Advances in the Cold Food Chain

(978-0-08-100308-4)

Lawrie’s Meat Science, 8th Edition

(978-0-08-100694-8)

Improving the Sensory and Nutritional Quality of Fresh Meat, 2nd Edition

(978-0-08-100-720-4)

Copyright

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This book and the individual contributions contained in it are protected under copyright by the Publisher (other than as may be noted herein).

Notices

Knowledge and best practice in this field are constantly changing. As new research and experience broaden our understanding, changes in research methods, professional practices, or medical treatment may become necessary.

Practitioners and researchers must always rely on their own experience and knowledge in evaluating and using any information, methods, compounds, or experiments described herein. In using such information or methods they should be mindful of their own safety and the safety of others, including parties for whom they have a professional responsibility.

To the fullest extent of the law, neither the Publisher nor the authors, contributors, or editors, assume any liability for any injury and/or damage to persons or property as a matter of products liability, negligence or otherwise, or from any use or operation of any methods, products, instructions, or ideas contained in the material herein.

Library of Congress Cataloging-in-Publication Data

A catalog record for this book is available from the Library of Congress

British Library Cataloguing-in-Publication Data

A catalogue record for this book is available from the British Library

ISBN: 978-0-08-100593-4 (print)

ISBN: 978-0-08-100600-9 (online)

For information on all Woodhead publications visit our website at https://www.elsevier.com/books-and-journals

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Typeset by Thomson Digital

List of Contributors

J.L. Aalhus,     Agriculture and Agri-Food Canada, Lacombe, AB, Canada

D.T. Berhe,     University of Copenhagen, Copenhagen, Denmark

H.C. Bertram,     Aarhus University, Graasten, Denmark

S. Bonny

Murdoch University, Murdoch, WA, Australia

INRA, UMR1213 Herbivore, Saint Genès Champanelle

Clermont Université, VetAgro Sup, UMR1213 Herbivore, Saint Genès Champanelle, France

H.L. Bruce,     University of Alberta, Edmonton, AB, Canada

B.P. Dalrymple

CSIRO Agriculture, Brisbane, QLD

The University of Western Australia, Perth, WA, Australia

C.J.S. De Backer,     University of Antwerp, Antwerp, Belgium

L.O. Dragsted,     University of Copenhagen, Frederiksberg, Denmark

B. Egelandsdal,     Norwegian University of Life Sciences, Aas, Norway

E.M. England,     The Ohio State University, Columbus, OH, United States

M. Enser,     University of Bristol, Bristol, United Kingdom

M. Estévez,     University of Extremadura, Cáceres, Spain

L. Faucitano,     Agriculture and Agri-Food Canada, Sherbrooke, QC, Canada

D. Frank,     CSIRO Food & Nutrition, Sydney, NSW, Australia

M. Gagaoua

INRA, UMR1213 Herbivore, Saint Genès Champanelle

VetAgro Sup, UMR1213 Herbivore, Saint Genès Champanelle, France

Université Frères Mentouri Constantine, Constantine, Algeria

D.E. Gerrard,     Virginia Polytechnic Institute, Blacksburg, VA, United States

T. Grandin,     Colorado State University, Fort Collins, CO, United States

M.L. Greaser,     University of Wisconsin-Madison, Madison, WI, United States

B. Guo

Nanjing Agriculture University, Nanjing

Kemin Animal Nutrition & Health Division, China, Zhuhai, China

CSIRO Agriculture, Brisbane, QLD, Australia

W. Guo,     University of Wyoming, Laramie, WY, United States

M. Ha,     Melbourne University, Parkville, VIC, Australia

A. Haug,     Norwegian University of Life Sciences, Aas, Norway

M. Henchion,     Teagasc Food Research Centre, Dublin, Ireland

J.-F. Hocquette

INRA, UMR1213 Herbivore, Saint Genès Champanelle

Clermont Université, VetAgro Sup, UMR1213 Herbivore, Saint Genès Champanelle, France

K. Hollung,     Nofima AS, Tromsø, Norway

L. Hudders,     Ghent University, Ghent, Belgium

J. Hughes,     CSIRO, Brisbane, QLD, Australia

Ó. López-Campos,     Agriculture and Agri-Food Canada, Lacombe, AB, Canada

R. Lametsch,     University of Copenhagen, Copenhagen, Denmark

C. Lanusse,     UNCPBA, Tandil, Argentina

G. Martelli,     University of Bologna, Bologna, Italy

S.K. Matarneh,     Virginia Polytechnic Institute, Blacksburg, VA, United States

K. Matthews,     Agriculture and Horticulture Development Board (AHDB) Beef and Lamb, Kenilworth, United Kingdom

R. Miklos,     University of Copenhagen, Copenhagen, Denmark

L. Moreno,     UNCPBA, Tandil, Argentina

M.N. Nair,     University of Kentucky, Lexington, KY, United States

A. Namvar,     University of Guelph, Guelph, ON, Canada

E. Nannoni,     University of Bologna, Bologna, Italy

T. Nishimura,     Hokkaido University, Sapporo, Japan

N. Oksbjerg,     Aarhus University, Tjele, Denmark

M. Oostindjer,     Norwegian University of Life Sciences, Aas, Norway

Y. Oytam,     CSIRO Food & Nutrition, Sydney, NSW, Australia

J.E. Paulsen,     Norwegian University of Life Sciences, Oslo, Norway

P.C. Pereira,     CiiEM / Egas Moniz C.R.L., Monte de Caparica, Portugal

D. Pethick,     Murdoch University, Murdoch, WA, Australia

B. Picard

INRA, UMR1213 Herbivore, Saint Genès Champanelle

VetAgro Sup, UMR1213 Herbivore, Saint Genès Champanelle, France

R. Polkinghorne,     Farmer/Consultant, Murrurundi, NSW, Australia

M.J. Post,     Maastricht University, Maastricht, The Netherlands

E. Puolanne,     University of Helsinki, Helsinki, Finland

P.P. Purslow,     National University of Central Buenos Aires Province, Tandil, Argentina

M. Sødring,     Norwegian University of Life Sciences, Oslo, Norway

T.L. Scheffler,     University of Florida, Gainesville, FL, United States

N. Scollan,     Aberystwyth University, Aberystwyth, United Kingdom

A. Sikes,     CSIRO Food & Nutrition, Brisbane, QLD, Australia

P. Strydom

API-ARC, Irene

University of Stellenbosch, Stellenbosch, South Africa

S.P. Suman,     University of Kentucky, Lexington, KY, United States

M. Therkildsen,     Aarhus University, Tjele, Denmark

A. van Huis,     Wageningen University, Wageningen, The Netherlands

R. Vaskoska,     Melbourne University, Parkville, VIC, Australia

F. Vicente,     CiiEM / Egas Moniz C.R.L., Monte de Caparica, Portugal

R. Warner,     Melbourne University, Parkville, VIC, Australia

K. Warriner,     University of Guelph, Guelph, ON, Canada

E.C. Webb,     University of Pretoria, Pretoria, South Africa

E.M. Webb,     University of Pretoria, Pretoria, South Africa

T. Widowski,     University of Guelph, Guelph, ON, Canada

J.D. Wood,     University of Bristol, Bristol, United Kingdom

Acknowledgments

Any journey can be delightful if you travel with good companions. I am delighted to acknowledge the people who made the journey to completion of this book such a pleasure.

My thanks to Rob Sykes, Josh Bennett, and Karen Miller at Elsevier for their great professionalism and friendly help as acquisitions editor and editorial project managers.

Many thanks to all the contributors for sharing their great knowledge and experience. The content of this book is a product of their great expertise. If a person is judged by the company they keep, I am honored to be so judged.

Peter P. Purslow

Tandil, Argentina

Chapter 1

Introduction

P.P. Purslow    National University of Central Buenos Aires Province, Tandil, Argentina

Abstract

The set of properties that defines overall consumer perception of meat quality has expanded to include extrinsic factors, such as animal welfare, sustainability of production and meat in relation to human health, as well as the traditional factors intrinsic to the meat itself, such as color, flavor, and texture. This chapter explains the purpose of this book to cover what is new in traditional meat quality, new ways of prediction or measuring meat quality, and current consumer perceptions.

Keywords

meat quality definitions

extrinsic cues

color

flavor

tenderness

ethics

animal welfare

wholesomeness

1. What is meat quality?

Meat quality can be defined as a set of properties that together identify what we appreciate about meat when we purchase it, eat it, or select it for use as a raw material for processing into meat products. As our personal and communal preferences and appreciations change with changes in society, it is axiomatic that definitions of meat quality can also change.

Traditionally, the set of properties used to define the quality of meat intended for consumption as whole meat, rather than meat products, are those associated with our sensory perception; appearance, color, flavor, texture (especially tenderness), juiciness/water-holding, and odor. The other traditional quality factor, normally expressed as freshness or wholesomeness, relates to the perception that the meat is safe to eat, in terms of lack of pathogens, parasites, infections agents, or toxins. Although freedom from infections agents is an unseen quality, we associate it with freshness; meat that looks old to us is untrusted.

In the first-half of the 20th century, the provision of enough meat to feed people and the preservation of wholesomeness was the principal focus of meat science, and when a provision of wholesome meat was secure, the intrinsic set of quality parameters (i.e., those parameters that we could see, taste, smell, or feel) were the most important parameters used to judge meat at its point of purchase, or on consumption after cooking. Much of the work done on best practices for genetic selection, animal production, slaughter methods, and postmortem handling of meat aimed to minimize variability in these intrinsic meat quality parameters.

Above and beyond these intrinsic parameters, a further set of extrinsic parameters gained a prominent position in the minds of current consumers of meat and meat products. They are termed extrinsic because they cannot immediately be detected by physical or sensory examination of the meat itself, but are associated with the way that the meat is produced. These extrinsic factors center around animal welfare, the nutritional values of meat in the human diet, and the ecological sustainability of production systems. In other words, the well-being of meat animals, the well-being of meat consumers, and the well-being of society as a whole are now principal attributes of meat production systems and the final product itself. These attributes are discussed fully by Grunert (2005).

The balance among meat availability, wholesomeness, and intrinsic and extrinsic factors varies from country to country, depending on local customs and on the state of the local economy. In some developing countries, the price of meat and its availability or continuity of supply are the most important factors for consumers. When continuity of supply is secure, wholesomeness or freshness is the next major concern. If this is also satisfied then the traditional (intrinsic) eating qualities become important. We can thus view various attributes of meat quality in a form analogous to Maslow’s triangle of needs (Maslow, 1943), as depicted in Fig. 1.1. When each level of need is satisfied, it becomes less dominant and the next level up takes on more importance.

Figure 1.1   Consumer perceptions of meat quality represented as a triangle of needs, that is, that the more basic needs or desired quality elements at the bottom levels of the triangle need to be more or less satisfied before higher-level quality attributes become important.

In general, consumers in countries with a very high gross national product nowadays are most concerned with the issues of animal welfare, human health, and ecological sustainability of meat production. In high-income countries, there has been a tendency for meat consumption to fall, leading to the idea of an inverted U-shaped curve (or Engel curve) between personal income and meat consumption. However, this is strongly confounded by local cultures and customs; in many countries (e.g., Uruguay, Argentina), a high per capita meat consumption is maintained in all but the poorest families almost regardless of income, due to the central role of meat in the local food customs.

2. The aim and structure of this book

There is an existing range of fine textbooks covering the basic principles of meat science in relation to the traditional, intrinsic quality parameters, and the aim of this book is not to repeat or replace these. Rather, the aim is to extend the scope of topics covered by meat quality to give adequate coverage to extrinsic as well as intrinsic qualities. In the 21st century, the general understanding of what constitutes meat quality in the minds of consumers, marketers, and producers has changed. The purpose of this book is to encapsulate the modern understanding of meat quality and how it is built on the traditional strong science base.

The scope of the book is principally limited to meat consumed as whole cuts of muscle rather than processed meat products. This is because: (1) there is a range of recent texts that examine meat processing very well, and (2), the consumer perceptions of processed meats and questions about their nutritional value and role in human health is a vast topic on its own.

The book is divided into three themes and each theme is divided into topic chapters, each of which is written by eminent authorities with insight and experience on the individual topics. While the individual contributors are united in the thrust of the book, they each have their own styles, which I hope add to the richness and diversity of this book. In many chapters, concise text-boxes briefly highlight the interactions between different chapters in the book. These text-boxes represent the thoughts of the editor, and so the authors of each chapter must be exempt of blame for any errors in these.

Theme (1). What is new in our understanding of the association between muscle structure, the conversion of muscle to meat, and the intrinsic eating qualities of cooked meat, including food safety considerations?

This is a topic area where the fundamental mechanisms leading to variations in intrinsic meat quality are reasonably well understood and the basics are well described in existing meat science textbooks. I shall therefore take a little space to describe what is new in this part of the book, and why specific topics were chosen. The specific aim of the chapters in this theme is to update our current understanding, rather than reiterate the established basics. The exception to this rule is Chapter 2, which gives a concise overview of current knowledge on the structure and proteins of muscle, and serves as a prelude to the discussion of new advances in the following chapters in this theme. Chapter 3 continues with a review of myogenesis and muscle growth, with special emphasis on intrauterine growth and fetal programming as current areas of interest on how development affects meat quality. This is followed in Chapter 4 by a detailed look at the mechanisms controlling the conversion of muscle to meat postmortem, with attendant effects on the color, oxidation, texture, and water-holding capacity of meat. This chapter is important because it extends our understanding of these perimortal and postmortem biochemical events beyond a simple consideration of rates of pH change. The section on mitochondrial metabolism postmortem is intriguing as current views on programmed cell death, or apoptosis, consider that mitochondria are the main executioners of apoptosis (Estaquier et al., 2012), activating the caspase cascade which ultimately degrades cell functions.

This brings us neatly to discuss one of the topics that is not included in the book, and why it is omitted. The topic of postmortem proteolysis in meat and its relation to changes in qualities, such as water holding and cooked meat texture has been a central theme in the biochemical aspects of meat science for more than 50 years. There are four major systems of proteolytic enzymes within muscle cells and two major extracellular systems; the proteases within the muscle cells include the lysosomal cathepsins, the calpains, the ubiquitin-proteosome system, and the caspase system of the apoptotic process. Degradation of the extracellular matrix is principally by the matrix metalloproteinases (MMPs), but the ADAMs system of enzymes is also involved at the exterior surface of the muscle cell. The calpains and their inhibitor, calpastatin, have long been the focus of attention with regards to the development of tenderness postmortem (Koohmaraie, 1992; 1994; Koohmaraie and Geesink, 2006). Despite evidence that the proteasome system may be involved in meat tenderization (Lamare et al., 2002; Liu et al., 2016), this enzyme system has received relatively little attention in the meat science area, although it is known as the principal enzyme system involved in muscle degradation in vivo (Mitch and Goldberg, 1996). Since 2002 there has been growing interest in the role of the caspase system in the development of meat tenderness [as reviewed by Sentandreu et al. (2002); Kemp et al. (2010); Kemp and Parr (2012)]. Despite the recent interest in caspases, there is a sense that the study of proteolysis in relation to meat tenderization and to water holding has reached a mature phase. This influenced the decision not to include a further update on this topic in this section on recent developments, as the excellent reviews by Sentandreu et al. (2002), Huff-Lonergan and Lonergan (2005), Kemp et al. (2010), and Huff-Lonergan et al. (2010) appear to still capture the essence of current thinking in this area. A recent review of the significance of matrix metalloproteases to meat quality is also available (Christensen and Purslow, 2016).

This section of the book on what is new in our understanding of the association between muscle structure, the conversion of muscle to meat, and the intrinsic eating qualities of cooked meat continues with two somewhat related chapters, one on oxidation and the other on meat color. Oxidation of proteins and lipids in meat is a hot topic in relation to human health, and currently there is considerable research effort on antioxidant strategies, both in living animals and in treatment of meat. The chapter on meat color updates our basic knowledge of color chemistry as well as addressing current techniques for manipulation meat color by packaging.

Variability in the texture, and especially the tenderness, of meat has been an important concern of meat scientists for over a century, and the control and prediction of meat texture continues to be an important topic. As well as reviewing current thinking on the mechanisms controlling meat texture and current practices to measure this, the chapter on advances in meat texture addresses the continuing efforts of researchers to find reliable techniques to predict cooked meat texture from measurements on raw meat early postmortem. The identification of rapid and preferably nondestructive, techniques that could be used online in the slaughterhouse to predict the tenderness of the cooked product remains a holy grail objective.

The water holding in meat is a topic that has been researched and reviewed extensively. Chapter 9 presents an interestingly different slant on the topic from previous reviews; it highlights just how much the established theories of water holding can and cannot explain the phenomenology of the subject, and draws attention to those complexities of the system that have been overlooked by the application of theories attempting to simplify our understanding. In challenging the current theories, this chapter provides much food for thought.

Meat safety and microbiology is another huge topic whose history and current state of knowledge could hardly be reviewed in a single chapter, and Chapter 10 does not attempt to do so; rather, it takes the interesting path of reviewing the developments in our approaches to controlling food pathogens and the current focus on reducing pathogen loads from the living animals.

Part one of the book concludes with a fresh look at the international standards and methodology for assessing meat and carcase quality. It highlights the disparity of grading schemes in major meat markets and the growing movement toward globalization of these standards.

Theme (2). New techniques for measuring, predicting, or producing meat quality, and how they help us minimize variability in eating quality and/or maximize value.

The techniques chosen for discussion in the first part of this theme mainly relate to intrinsic meat qualities. This theme starts with a chapter on the transcriptomics of meat quality. (The transcriptome is the total set of all the RNA molecules that are found in meat; that is, the expressed products of the active genes in the tissue. The transcriptome is obviously the precursor of the proteome, the entire set of proteins found in the tissue.) The transcriptome represents only the products of the genome that are expressed in that tissue, and can vary with age, time, nutrition, and external stimuli. Genomics and transcriptomics of meat animals have made huge advances in the 21st century, but it is fair to say that the majority of this has been in relation animal growth, production efficiency, and meat yield. The focus of this chapter is on those aspects of transcriptomics which relate specifically to qualities of meat, such as color, water holding, and tenderness as well as intramuscular fat. Quite logically, this chapter on transcriptomics is followed by a chapter on proteomics in relation to meat (and fish) quality. As the authors of this chapter note, proteomics has been booming in the first years of the 21st century, and has been increasingly used to try and describe or predict a range of intrinsic meat quality attributes. Following on, the next chapter deals specifically with NMR spectroscopy as a technique in another -omics field, metabolomics. The metabolome is the total set of metabolites that occur in a particular tissue, and so reflects the entire physiology of the tissue. This chapter examines the recent progress in using NMR spectroscopy to study a range of metabolites left behind by cell processes in meat. It focuses on perimortal mebabolism, changes in meat during processing, and metabolomics studies of differences in species and species authenticity. This use of NMR spectroscopy included in this theme on new techniques is radically different from another use of NMR that has been with us for some time, which is relaxometry (i.e., the time-dependent change or deterioration of NMR signals with time). The use of NMR relaxometry to study water mobility in muscle tissue and meat is another area of meat science which can be said to have reached a mature phase, following a period of very active discoveries in the late 20th century and in the early 2000s. There are excellent reviews of NMR relaxation studies in meat by Bertram and colleagues (Bertram and Ersen, 2004; Bertram et al., 2006; Bertram and Andersen, 2007) and Pearce et al. (2011). Because of this mature phase and the existence of excellent reviews, NMR relaxometry is not given a separate chapter in this book, although there is some discussion of it in the chapter on water holding.

Another technique that has enjoyed considerable success in predicting many aspects of meat quality in near infra-red spectroscopy. Again, this is a mature research area with about 30 years of development. Prieto et al. (2009) comprehensively review the application of this technique to the prediction of meat quality. A related technique is hyperspectral imaging (where information across the spectrum is obtained from each pixel in an image). There are several recent reviews of the use of hyperspectral imaging to predict several aspects of meat quality (ElMasry and Sun, 2010; ElMasry et al., 2012; Xiong et al., 2015) and the techniques are now sufficiently robust that practical application in the meat industry are forthcoming. Again, because of the maturity of the NIR spectroscopy field and the presence of excellent reviews on this and on hyperspectral imaging, it was decided that there was little point in reviewing them again here.

The cooking of meat can hardly be described as a new technique, and the changes in meat and meat proteins have been extensively investigated in the past. However, it is fair to say that, although the phenomenology of changes in meat color, texture, and water holding on heating are well-understood, there is still a surprising lack of really rigorous information on the exact mechanisms behind many of those changes. Chapter 14 describes new approaches to studying changes in the macroscopic and molecular changes in meat during heating using X-ray phase-contrast tomography [as opposed to the more familiar X-ray based computer tomography (CT) scanning, which produces image contrast due to differences in absorption of X-rays] and by Raman spectroscopy. Following on, Chapter 15 looks at innovative cooking and processing technologies to improve meat texture. It provides insight into the processes of ohmic heating, high pressure processing, shockwave, ultrasound, pulsed electric field, Smartstretch, and sous vide cooking that can modify meat tenderness, and sets these against a background of an updated synopsis of the effects of conventional cooking regimes.

Within this theme we also discuss new paradigms for the production of sufficient animal proteins to feed the growing global population, outside the conventional patterns of production that currently exist. The potential (and some of the problems) of alternative animal protein production by cultured meat (meat grown in vitro using cell culture techniques) is discussed in Chapter 16 and the use of edible insects as an alternative to the global demand for protein follows on in Chapter 17. Questions of sustainable production and global responsibility are strong elements in these chapters. The first represents a high-technology approach to producing meat proteins, while the second represents a more pragmatic approach of exploiting existing species. There are obviously questions of consumer attitudes to both the production of cultured meat and to the eating of insects or proteins extracted from them.

Theme (3). The current qualities of consumer and public perceptions; what is sustainable, ethical, desirable, and healthy.

The third and final theme in this book takes a detailed look at extrinsic meat quality cues. It focuses on current consumer and public perceptions; what is sustainable, ethical, desirable, and healthy in terms of meat production, slaughter, and postmortem treatment of meat from the viewpoint of society and the consumer. New aspects of sensory perceptions of consumers are discussed here. This theme includes the issue of drug residues in meat, a result of modern production practices that concerns many consumers.

The impacts of meat consumption on human health is one of the most prominent issues highlighted by the media in recent times. Theme three starts by considering aspects of the important but highly complex issue of the nutritive value of meat and its impact on human health in Chapter 19. This is followed by a very careful examination of the relationship between meat consumption and cancer in Chapter 20. These two carefully-argued chapters contribute a level of analysis that cuts through some of the more sensational statements in the popular media. The healthy food aspect is rounded out in Chapter 21 by consideration of the fatty acid composition of meat, another prominent consumer issue, and how this can be manipulated in both ruminants and mongastric meat species by the manipulation of animal diets.

The next two chapters deal with another issue of great importance in consumer perceptions of the meat industry, which is animal welfare. Chapter 21 provides a detailed review of the fundamentals of animal welfare in modern production systems and also contrasts the attitudes of consumers in Europe versus North America toward animal welfare issue in meat production. Chapter 22 gives an entirely different take on animal welfare issues by discussing the personal experiences of an animal welfare expert in working with large companies to improve animal welfare in practice in the meat industry.

Another major concern of modern consumers of meat is the possibility that residues of antibiotics, growth promoters, hormones, and other drugs given to animals in the production process may end up in the meat they consume. We devote two full chapters to this issue, first outlining in Chapter 23 the general principles of drug residues in meat and the means of controlling these, and in Chapter 24 giving specific examples of those pharmacological agents most commonly evaluated.

We then move on to the topic of ethics in meat production (Chapter 24) and the acceptability of production and processing procedures in the minds of consumers. This topic is extended further in Chapter 25 with a review on consumer perceptions on ethical and sustainable production, and systems credibility. Finally, Chapter 26 gives a final overview of what consumers perceive to be ethical, sustainable, healthy, and desirable while also stressing the sensory perceptions of individual consumers.

Although each chapter can be viewed as a stand-alone resource, it is intended that the book as a whole provides a modern view of what is changing in our perception of meat quality.

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Bertram HC, Ersen HJ. Applications of NMR in meat science. Annu. Rep. NMR Spectrosc. 2004;53:157–202.

Bertram HC, Wu Z, van den Berg F, Andersen HJ. NMR relaxometry and differential scanning calorimetry during meat cooking. Meat Sci. 2006;74:684–689.

Christensen S, Purslow PP. The role of matrix metalloproteinases in muscle and adipose tissue development and meat quality: a review. Meat Sci. 2016;119:138–146.

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ElMasry G, Barbin DF, Sun DW, Allen P. Meat quality evaluation by hyperspectral imaging technique: an overview. Crit. Rev. Food Sci. Nutr. 2012;52:689–711.

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Part I

Developments in Our Understanding the Association Between Muscle Structure and the Basic Eating Qualities of Cooked Meat

Chapter 2: Muscle Structure, Proteins, and Meat Quality

Chapter 3: Myogenesis and Muscle Growth and Meat Quality

Chapter 4: Perimortal Muscle Metabolism and its Effects on Meat Quality

Chapter 5: What’s New in Meat Oxidation?

Chapter 6: Current Developments in Fundamental and Applied Aspects of Meat Color

Chapter 7: Advances in the Understanding and Measurement of Meat Texture

Chapter 8: Developments in Our Understanding of Water-Holding Capacity in Meat

Chapter 9: Current Challenges in Enhancing the Microbiological Safety of Raw Meat

Chapter 10: Quality Assurance Schemes in Major Beef-Producing Countries

Chapter 2

Muscle Structure, Proteins, and Meat Quality

W. Guo*

M.L. Greaser**

*    University of Wyoming, Laramie, WY, United States

**    University of Wisconsin-Madison, Madison, WI, United States

Abstract

Muscle is a major source of protein consumed by humans. With currently more sufficient food supplies, meat quality and meat tenderness becomes increasingly important to meet consumer’s requirement. Meat tenderness is associated with many factors involving structural changes of muscle, protein degradation, breakdown of high-energy compounds, enzyme activity, pH, temperature, and processing time. It also varies between species and breed, between different muscles, and at different distances from the muscle surface because of temperature gradients during the conversion of muscle to meat. This chapter summarizes skeletal muscle structure and contractile function, protein degradation, enzyme changes, and changes of muscle-associated connective tissues postmortem. Furthermore, examples that discuss their effects on meat tenderness have been given. Although advanced research and technologies have been applied to improve meat quality, some of the mechanisms involved in conversion of muscle to meat still remain to be determined.

Keywords

muscle

meat quality

meat tenderness

muscle proteins

muscle structure and contractile function

1. Introduction

Muscles facilitate locomotion of and support to the body. They are composed of three distinct types: skeletal, cardiac, and smooth muscles. Among these three types, skeletal and cardiac muscles are also called striated muscle due to the visible stripes on the surface of the muscle fibers or cells when observed under a microscope. All three types of muscles are used in meat products. In terms of conversion to meat, skeletal muscles are the most important tissue of these three types because of quantity and economic value. This chapter therefore summarizes our understanding mainly of the structure and function of skeletal muscles, their structural components, and their behavior postmortem. Detailed information regarding these topics has been covered in several excellent reviews and book chapters (Bagshaw, 1993; Bendall, 1973a; Brooks, 1998; Engel and Franzini-Armstrong, 1994; Greaser, 1986; Greaser and Pearson, 1999; Hochachka, 1999; Lawrie, 1992; Matthews, 1998; Richter et al., 1998; Xiong et al., 1999).

2. Structure and function of muscle

2.1. Macrostructure

Skeletal muscle is the largest edible portion of all meat animal species including cattle, sheep, pigs, and chicken. There are approximately 500–800 muscles in most animals, including humans. The form of a muscle is determined by its function. To increase the amount of force or power, more fibers or fibers with larger diameter are needed. Strap or fusiform muscles are specialized for speed; pennate muscles can produce more power. The speed of a muscle fiber (and the collective mixture of a whole muscle) is determined by the intrinsic property of the nerves that control it. The range of movement depends on the muscle length. For intact to near-intact muscle foods, it is important to understand the morphological muscle type as this may impact the tenderness.

Series-Fibered Muscles

Typical descriptions of skeletal muscles depict the individual fibers as running the length of a fascicle, terminating in a myotendinous junction at each end. However, in approximately 50% of muscles in birds, amphibians, and mammals (with the exception of humans and great apes), muscle fibers are much shorter than fascicles and terminate intrafascicularly with no direct attachment to the tendon (Trotter et al., 1995). In these series-fibered muscles, force is transmitted through the endomysium that connects them. For example, the pectoralis (breast) muscle of all birds studied (including chicken, duck, goose, turkey, and other species used as game or poultry meat) has short (1.5-cm long) fibers arranged in series.

Anatomically, skeletal muscle is encased in several layers of connective tissue and contains other tissue types (nerves, blood vessels, fat cells, and capillaries) (Fig. 2.1). Each individual muscle is usually attached to the skeleton or bone by a tough, nearly inextensible connective tissue layer called the epimysium. The epimysium is the outermost layer of connective tissue. Within this connective tissue sheath, a group of fascicles or muscle bundles (secondary bundle) is surrounded by connective tissue known as the perimysium. Within each fascicle, approximately 20–40 muscle fibers form the primary bundle. Each fiber is separated by the endomysium, which is directly attached to the muscle cell membrane. The epimysium, perimysium, and endomysium contain mainly the collagen fibers that intermesh to transmit contractile force from the cell level to bones or other tissues for movement of the body. This connective tissue (or extracellular matrix) is considered to be a major determinant of meat tenderness and changes with age.

Figure 2.1   Diagram of a muscle cross-section. (Modified from Ham, A.W., 1965. Histology, fifth ed. J.B. Lippincott Company, Philadelphia. Used by permission.)

2.2. Microstructure

At the cellular and molecular levels, the skeletal muscle cells or fibers are unique in that they are multinucleate, very large, and extremely elongated, reaching several millimeters to centimeters in length. The muscle cell includes an outer cell membrane called the sarcolemma, the T-tubules, sarcoplasmic reticulum (SR), mitochondria, and myofibrils (Fig. 2.2). T-tubules are not real organelles but rather perpendicular extensions of the sarcolemma that extend through the center of the cell. SR surrounds each myofibril and is the site of calcium storage and release. It regulates the calcium ion concentration in the cytosol. Mitochondria are the sites of oxidative metabolism in the cell. The number and location of mitochondria vary greatly between muscle types. In white skeletal muscle, they occupy about 2% of the volume, while they make up 34–38% of the volume of cardiac muscle cells. Their concentration is greater near the sarcolemma than in the interior parts of the cell.

Figure 2.2   Diagram showing the microstructure of a muscle fiber. (Modified from Greaser, M.L., Guo, W., 2012. Post-mortem muscle chemistry. In: Hui, Y.H. (Ed.), Handbook of Meat and Meat Processing, second ed. CRC Press, Boca Raton, FL, pp. 70–78.)

Myofibrils occupy about 80% of the cell volume in the skeletal muscle cell. There are typically 500–1000 myofibrils in the cross-section of a skeletal muscle fiber. Myofibrils facilitate the major function of the muscle fiber, whereby they produce force when skeletal or cardiac muscles contract. They are not bounded by a membrane and consist entirely of proteins that exist as an insoluble structure at physiological salt concentrations. The structure of the myofibril is string-like and is composed of repeated sarcomeres that represent the smallest contractile unit of muscle. One sarcomere unit is located between two adjacent Z-lines. The Z-line (also called Z-disk) is composed primarily of the protein α-actinin. Thin filaments containing primarily the protein actin attach to the Z-line in opposite directions. The I-band is bisected by a dark Z-line located at the center of the I-band. Thick filaments, containing primarily the protein myosin, are located in the center of the sarcomere forming the broad dark A-band. The M-line is a dark line in the very center of A-band. The arrangement of thin and thick filaments gives the skeletal and cardiac muscle cells a striated appearance, where the lighter region has only thin filaments (I-band), the darkest region contains the thick filaments (A-band), and the less dark region has only thick filaments (H-zone) (Fig. 2.2) (Swartz et al., 2009). Understanding the banding pattern in myofibrils is important because the lengths of the sarcomere are related to meat tenderness.

A third filament type also runs through the sarcomere and is solely composed of the protein titin. This giant protein plays a critical role in the structural formation of the sarcomere even though it is still controversial as a protein ruler for thick filament length control (Kontrogianni-Konstantopoulos et al., 2009; Tskhovrebova and Trinick, 2012; Granzier et al., 2014; Tskhovrebova et al., 2015). Its amino terminus anchors in the Z-line and overlaps another titin’s amino terminus from an adjacent sarcomere (Furst et al., 1988; Labeit and Kolmerer, 1995; Trinick and Tskhovrebova, 1999; Obermann et al., 1996; Gregorio et al., 1998). Its extensible elements—N2B, middle Ig, and PEVK—are located in the I-band; the rest of the titin molecule runs through the half A-band. Its carboxyl terminus anchors in the M-line and overlaps another titin’s carboxyl terminus from the adjacent half sarcomere. Titin thus constitutes a continuous filament system along the myofibril. Titin binds to both actin and myosin filaments at I-band and A-band, respectively, preventing overstretching of muscle, aligning actin and myosin, maintaining thick filaments in the center of the sarcomere, and producing passive tension (Fig. 2.2) (Tskhovrebova and Trinick, 2003; Granzier and Labeit, 2004; Horowits et al., 1986; Guo et al., 2010). Postmortem change of titin has also been proposed to be associated with meat tenderness. In addition to titin, postmortem change of the proteins forming a cytoskeletal network such as filamin, vinculin, desmin, talin, synemin, and dystrophin is also an important contributor to meat tenderness. The detailed mechanisms have been discussed in previous studies (Taylor et al., 1995; Greaser, 1991; Bilak et al., 1998; Evans et al., 1984; O’Shea et al., 1979; Schmidt et al., 1999; Huff-Lonergan and Lonergan, 2005; Koohmaraie et al., 2002).

2.3. Contraction Mechanism

Skeletal muscle contraction is a complicated process of molecular interactions between peripheral nerves and skeletal muscle cells. It is necessary to understand this because many of the metabolic processes postmortem are attempting to keep muscle in a state ready for the activation of contraction. Activation of contraction of a skeletal muscle cell is the precise process by which the neural activation culminates in muscle contraction known as excitation–contraction coupling (EC coupling) (Ebashi et al., 1980). EC coupling starts with a nerve impulse that transports the action potential down the axon to a specialized region on the muscle cell termed the motor end plate. The neurotransmitter acetylcholine (ACh) is then released from the end of the axon and binds to ACh receptors on the muscle cell membrane, resulting in opening of the receptor’s Na+ channel and consequent local membrane depolarization. This depolarization wave spreads along the sarcolemma and down the T-tubules. The T-tubules are attached to a specialized intracellular membrane system called the SR. Depolarization of T-tubules is sensed by the calcium release channel [composed mainly of the ryanodine receptor (RyR)] of the junctional SR. The calcium channel then opens and calcium is released from the lumen of the SR into the cell cytosol. Released calcium in the region of the myofilaments then triggers the contraction cycle of muscle cell. This cycle involves the major contractile proteins (actin and myosin) and regulatory proteins [troponins and tropomyosin (TM)] either directly or indirectly (Fig. 2.3).

Figure 2.3   Diagram showing the muscle contraction cycle.

ADP, Adenosine diphosphate; ATP, adenosine triphosphate; EC, excitation–contraction; RyR, ryanodine receptor; SR, sarcoplasmic reticulum.

The arrangement of thin and thick filaments has been discussed in Section 2.2. Thick filaments are mainly composed of the protein myosin, an asymmetric dimer composed of a globular head portion (S1), a hinged stalk region (S2), and a rod section. The S1 portion of myosin contains both the adenosine triphosphate (ATP) hydrolysis domain and the actin-binding domain (de Tombe, 2003). In addition to actin, the thin filament is also composed of TM and the troponin complex [troponin T (TnT), troponin C (TnC), and troponin I (TnI)] (Greaser and Gergely, 1971). The troponin complex binds to both actin and TM. TnC binds to TnI that attaches to TnT, TM, and actin, while TnT binds to TM. When calcium diffuses into the myofilaments and binds to the N-terminal regulatory domain of TnC, calcium causes a conformational change in the troponin complex, causing the TnC:TnI association to strengthen while at the same time weakening the TnI:TnT association. This conformational change results in the movement of TM to expose a binding site for the heads of the myosin on the surface of the actin. This allows for cross-bridge formation, in which the myosin binds and pulls or pushes the actin a small distance (about 10 nm), and then the myosin head releases and reattaches to another actin. This sliding of the myofilaments is driven by the energy provided from ATP hydrolysis (Fig. 2.3) (Greaser and Guo, 2012; Gordon et al., 2000; Yin et al., 2015). When the impulses cease, the calcium is pumped back into the SR by the SR calcium-activated adenosine triphosphatase enzyme (Ca²+-ATPase) known as SERCA that is embedded within the SR membrane and one of the best understood ion transport enzymes (Entman and Van Winkle, 1986). This results in the calcium level dropping in the cytosol. With lower calcium levels, actin–myosin interaction is prevented, leading to muscle cell relaxation. This relaxation process is energy dependent and requires ATP. One cycle of muscle contraction and relaxation occurring after a single nerve depolarization pulse is called a twitch, and it takes only approximately 200 ms.

3. Muscle protein changes and meat quality

Although meat is composed of distinct tissues such as adipose, epithelial, connective, and nervous tissues, the major component of meat is muscle. The process of change between muscle and meat is complex and involves changes in the ultrastructure and proteins that are associated with meat quality. When an animal is dead, there are no new supplies of oxygen, nutrients, and energy for muscle function. On the other hand, the metabolism continues for some time in the muscle tissue, but the metabolites cannot be removed and they accumulate in the tissue, which leads to alterations of the muscle proteins and structure. The purpose of this section is to detail the proteins and structure changes in the muscle such as myofibril, organelles, membrane, and metabolic enzymes. Since connective tissue is one of the major factors to meat tenderness, this tissue is also discussed in this section.

3.1. Contractile Organelles

The contractile organelles are also known as myofibrils. The myofibril is an insoluble structure at near-physiological salt level that is composed of more than 30 different proteins. The major proteins and their approximate levels in the myofibrils are listed in Table 2.1. The striations appear within the myofibril due to the arrangement of myofibrillar proteins as discussed in Section 2.2, and the contraction mechanism has been discussed in Section 2.3. When the supply of ATP is depleted, the actomyosin bonds cannot be disassociated and become essentially permanent with this final state being referred to as rigor mortis. If muscle is unrestrained during ATP depletion, the sarcomere length may become shorter and thus influence the water-holding capacity and meat tenderness. Increased postmortem degradation of the myofibrillar proteins has also been associated with meat tenderness (Huff-Lonergan et al., 1996).

Table 2.1

Major Myofibrillar (MF) Proteins

Adapted from Swartz, D.R., Greaser, M.L., Cantino, M.E., 2009. Muscle structure and function. In: Du, M., McCormick, R.J. (Eds.), Applied Muscle Biology and Meat Science. CRC Press, Boca Raton, FL, pp. 1–40.

MF, Microfiltered; MW, molecular weight.

The proteins desmin, TnT, titin, nebulin, and vinculin all have been shown to be partially or completely degraded during the first week postmortem (Boehm et al., 1998). The proteolytic mechanisms responsible for this postmortem protein degradation have not been fully explained, but the endogenous sarcoplasmic calpain enzyme system is believed to play a major role. The calpains are calcium-activated proteases originally described by Dayton et al. (1976). The calpain system includes four major proteins in muscle: μ-calpain (calpain 1), m-calpain (calpain 2), p94 calpain (calpain 3), and calpastatin. Calpain 1 requires micromolar calcium concentrations for activity, while calpain 2 needs millimolar concentrations to be activated. Calpains 1 and 2 are ubiquitous in all cell types; in other cells they are responsible for continuously remodeling the cytoskeleton so as to allow cell movement. The calpain 3, a skeletal muscle-specific protease, is slightly larger than calpains 1 and 2. The role of calpain 3 in protein degradation remains poorly understood. Due to its rapid and thorough autolytic activity, it has not been isolated from muscle in an enzymatically active form. The fourth protein calpastatin is the inhibitor of calpains 1 and 2. The single nucleotide polymorphisms (SNPs) in the calpastatin and calpain genes have been associated with meat tenderness (Page et al., 2002; 2004; Schenkel et al., 2006; Casas et al., 2006; Barendse et al., 2007; Costello et al., 2007; Allais et al., 2011; Calvo et al., 2014). The activity of the calpain system relies on many factors including pH, temperature, and calcium concentrations (Steen et al., 1997; Goll et al., 2003). Their activity is compromised by the low pH and high ionic strength conditions during postmortem storage (Huff-Lonergan et al., 1996; Maddock et al., 2005). The earlier appearance of autolysis of ubiquitous calpains is thought to be associated with an earlier degradation of myofibrillar protein (Melody et al., 2004). High activity of the calpains induces high cleavage of specific myofibrillar proteins such as titin, desmin, and vinculin, leading to improvement of meat tenderness, while high levels of their inhibitor calpastatin are associated with decreased proteolysis and meat tenderness (Kemp et al., 2010; Kent et al., 2004). Among the calpains, calpain 1 has the most significant role in postmortem proteolysis and meat tenderization. The autolysis of calpain 1 in postmortem muscle has been used to indicate its prior activity (Melody et al., 2004; Kemp et al., 2010; Geesink et al., 2006). The calpains have the maximal activity at near pH 7, so they would be expected to have lower activation with pH decrease and at the ultimate pH of approximately 5.5. The activity of calpain 1 declines rapidly postmortem, while calpain 2 shows more stability (Bendall, 1973a). Interestingly, calpastatin levels also decline postmortem, so it is unknown which of these proteases are most important in controlling postmortem protein degradation. Initially, calpain 3 binds to the myofibrillar protein titin and influences proteolysis of titin and nebulin resulting in improvement of meat tenderization (Melody et al., 2004; Ilian et al., 2001, 2004a,b,c). However, the role of calpain 3 in postmortem meat tenderization is still controversial (Geesink et al., 2005). In addition to the calpain system, cathepsins may also play a role in myofibril protein degradation in postmortem muscle. Due to space limitation, the details will not be discussed here.

3.2. Metabolic Enzymes

ATP is the major high-energy small molecular compound in cells, and plays a critically important role in a large variety of metabolic activities. In muscle cells, ATP level is crucial for muscle metabolism and function (Fig. 2.4). ATP is produced by glycolytic, oxidative, and creatine phosphate (CP) pathways, while it is split predominantly by myosin-ATPase and SR Ca-ATPase. The plasmalemma Ca-ATPase, the plasmalemma Na+, K+-ATPase, and the mitochondrial ATPase might contribute to the ATP turnover in a minor way in postmortem muscle. Since the SR controls the cytosolic calcium concentration, the SR Ca-ATPase is clearly intertwined with the myosin-ATPase in the muscle contractile function described previously. ATP splitting through the ATPase enzyme system generates adenosine diphosphate (ADP) and inorganic phosphate, which are key substrates for glycolysis to proceed.

Figure 2.4   Overview of metabolism of muscle.

ATP, Adenosine triphosphate; CP, creatine phosphate. (Modified from Greaser, M.L., Guo, W., 2012. Post-mortem muscle chemistry. In: Hui, Y.H. (Ed.), Handbook of Meat and Meat Processing, second ed. CRC Press, Boca Raton, FL, pp. 70–78.)

After exsanguination, the blood supply ceases, leading to oxygen and new glucose cutoff; thus, the oxidative pathway is halted. Without mitochondrial ATP production, glycolysis of the glycogen stores becomes the primary way that ATP can be resynthesized. In aerobic glycolysis, muscle glycogen is further metabolized to pyruvate. Without an oxygen supply, the pyruvate cannot enter into the tricarboxylic acid (TCA) or Krebs cycle for further oxidation to produce more ATP. Furthermore, the pyruvate is metabolized to the end product lactic acid. In postmortem muscle, the products of metabolism can no longer be removed from the muscle, and thus lactic acid accumulates in the muscle tissue. This postmortem metabolism continues until glycogen and ATP are depleted. This process results in an overall pH decline to an ultimate pH of about 5.4–5.7. Since all the enzymes catalyzing the various steps in ATP producing and splitting are sensitive to pH as well as temperature, the postmortem muscle storage affects the activity of these enzymes in many different ways including preparations and species, and ultimately meat quality. For example, the activity of the myofibrillar ATPase depends on the muscle pH. Bentler (1977) found a distinct minimum in activity near pH 6.7 and declining activity below 5.8 with beef myofibrils. The minimum was less distinct in pig myofibrils. This pH 6.7 minimum correlates well with the minimum in ATP turnover described by Bendall (1973a,b). The temperature at which muscle is held postmortem also has an effect on the myofibrillar ATPase activity. In rabbit muscle held at 37°C, the Ca²+, Mg²+-ATPase activity declined by ∼25% within 6 h (Ikeuchi et al., 1980). Pig muscle myofibrils prepared from muscle held 8 h at 37°C had lost ∼75% of the ATPase activity compared to preparations made at death (Galloway and Goll, 1967). However, glycolytic enzyme activity remains relatively stable down to pH 5.5.

In addition to the glycolytic pathway in postmortem muscle, an additional backup source of ATP can be provided by CP (Fig. 2.4), an alternative high-energy phosphate store. The enzyme creatine kinase or phosphokinase catalyzes the reaction of ADP plus CP to generate ATP plus creatine (C) (Eq. (2.1)). This is a dynamic reaction in which higher levels of ATP and C generate ADP and CP in the reverse direction, and vice versa. The transfer of the phosphate from CP to ATP catalyzed by creatine kinase is very rapid so that the alteration of ATP level cannot be detected during a twitch. However, in postmortem muscle, creatine kinase is one of the enzymes most sensitive to postmortem denaturation. This enzyme is fairly stable down to pH 6.1 at 30°C but is rapidly inactivated at below pH 6.0 (Scopes, 1965). For example, Tarrant and Mothersill (1977) showed that this enzyme had a 12% loss in activity at 48 h postmortem in beef muscle at 1.5 cm from the surface but an 84% loss at 8-cm depth, suggesting that the high temperature in the deep

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