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Improving the Flavour of Cheese
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Commencer à lireLongueur: 1,141 pages19 heures
- Éditeur:
- Elsevier Science
- Sortie:
- Apr 30, 2007
- ISBN:
- 9781845693053
- Format:
- Livre
Description
Flavour is key to the acceptance of cheese products among consumers and is therefore a critical issue for professionals in the dairy industry. However, the manufacture of cheeses that are consistently safe and flavourful often eludes scientists. Developments such as high throughput genome sequencing and metabolite analysis are having a significant impact on research, leading to the development of new tools to control and improve the flavour of cheese. With contributions from an international array of acclaimed authors, Improving the flavour of cheese, provides crucial reviews of recent research in the field.
The book begins with a summary of cheese ripening and the compounds associated with cheese flavour. Part one discusses the metabolism of specific substrates to flavour compounds by microbes associated with milk and cheese. Part two reviews the influence of ingredients, processing and certain chemical and physical factors on cheese flavour. Part three addresses the measurement of cheese flavour. The book concludes with a selection of case studies on specific product types such as hard Italian, brined cheese, as well as low fat and soft-ripened cheeses.
Improving the flavour of cheese provides a unique review of emerging techniques and ideas to control the flavour of cheese. This original book will be a standard reference for those concerned with the development and manufacture of cheese. Discusses the wealth of research in the area of flavour development Reviews the influence of ingredients, processing and certain chemical and physical factors on cheese flavour Concludes with a selection of case studies on specific product types
The book begins with a summary of cheese ripening and the compounds associated with cheese flavour. Part one discusses the metabolism of specific substrates to flavour compounds by microbes associated with milk and cheese. Part two reviews the influence of ingredients, processing and certain chemical and physical factors on cheese flavour. Part three addresses the measurement of cheese flavour. The book concludes with a selection of case studies on specific product types such as hard Italian, brined cheese, as well as low fat and soft-ripened cheeses.
Improving the flavour of cheese provides a unique review of emerging techniques and ideas to control the flavour of cheese. This original book will be a standard reference for those concerned with the development and manufacture of cheese. Discusses the wealth of research in the area of flavour development Reviews the influence of ingredients, processing and certain chemical and physical factors on cheese flavour Concludes with a selection of case studies on specific product types
Informations sur le livre
Improving the Flavour of Cheese
Longueur: 1,141 pages19 heures
Description
Flavour is key to the acceptance of cheese products among consumers and is therefore a critical issue for professionals in the dairy industry. However, the manufacture of cheeses that are consistently safe and flavourful often eludes scientists. Developments such as high throughput genome sequencing and metabolite analysis are having a significant impact on research, leading to the development of new tools to control and improve the flavour of cheese. With contributions from an international array of acclaimed authors, Improving the flavour of cheese, provides crucial reviews of recent research in the field.
The book begins with a summary of cheese ripening and the compounds associated with cheese flavour. Part one discusses the metabolism of specific substrates to flavour compounds by microbes associated with milk and cheese. Part two reviews the influence of ingredients, processing and certain chemical and physical factors on cheese flavour. Part three addresses the measurement of cheese flavour. The book concludes with a selection of case studies on specific product types such as hard Italian, brined cheese, as well as low fat and soft-ripened cheeses.
Improving the flavour of cheese provides a unique review of emerging techniques and ideas to control the flavour of cheese. This original book will be a standard reference for those concerned with the development and manufacture of cheese. Discusses the wealth of research in the area of flavour development Reviews the influence of ingredients, processing and certain chemical and physical factors on cheese flavour Concludes with a selection of case studies on specific product types
The book begins with a summary of cheese ripening and the compounds associated with cheese flavour. Part one discusses the metabolism of specific substrates to flavour compounds by microbes associated with milk and cheese. Part two reviews the influence of ingredients, processing and certain chemical and physical factors on cheese flavour. Part three addresses the measurement of cheese flavour. The book concludes with a selection of case studies on specific product types such as hard Italian, brined cheese, as well as low fat and soft-ripened cheeses.
Improving the flavour of cheese provides a unique review of emerging techniques and ideas to control the flavour of cheese. This original book will be a standard reference for those concerned with the development and manufacture of cheese. Discusses the wealth of research in the area of flavour development Reviews the influence of ingredients, processing and certain chemical and physical factors on cheese flavour Concludes with a selection of case studies on specific product types
- Éditeur:
- Elsevier Science
- Sortie:
- Apr 30, 2007
- ISBN:
- 9781845693053
- Format:
- Livre
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Improving the Flavour of Cheese
acceptance.
1
Cheese manufacture and ripening and their influence on cheese flavour
P.L.H. McSweeney University College, Cork, Ireland
1.1 Influence of cheese manufacture on ripening and quality
‘Cheese is made in the vat.’ This traditional, and superficially obvious, saying contains an important element of truth: that the ripening of rennet-coagulated cheeses, and hence their flavour, texture and quality, are largely predetermined by the manufacturing process. The cheesemaker can vary only time, temperature and relative humidity/packaging during ripening, while many important factors which influence cheese ripening such as moisture content, levels of NaCl, pH, the cheese microflora and physical size of the cheese are influenced by manufacture. Indeed, it is difficult, and often impossible, to remedy during the maturation stage any mistakes made during curd manufacture. Hence, it is useful first to discuss cheese manufacture and how this process can influence ripening. Technological and scientific aspects of cheese manufacture have been described by many authors, including Kosikowski and Mistry (1997), Robinson and Wilbey (1998), Fox et al. (2000) and Fox and McSweeney (2004).
The manufacture of rennet-coagulated cheeses is essentially a dehydration process in which the fat and casein in the milk are concentrated 6- to 12-fold, depending on the variety. As shown in Fig. 1.1, the principal operations in cheesemaking are preparation of the cheesemilk (usually pasteurization and standardization), acidification by selected strains of lactic acid bacteria (LAB) known as starters, rennet coagulation, syneresis of the coagulum (which is controlled by factors such as cutting, stirring the curds/whey mixture, cooking and pressing), pressing and shaping the curds, and salting, although manufacturing protocols for particular groups of varieties (particularly Cheddar-type cheeses and pasta-filata varieties) have other operations such as controlled acidification and texturization of the curd and/or heating and stretching the curds in hot water.
Fig. 1.1 The major processes and events occurring during cheese manufacture and ripening.
Cheese manufacture commences with the selection of milk of the highest quality available. Since milk in countries with a developed dairy industry is now usually stored at refrigeration temperatures prior to processing, the microflora of raw milk is usually dominated by psychrotrophic organisms which can produce heat-stable proteinases and lipases (Suhren, 1988; Kroll, 1988) that at high cell counts (>10⁶ cfu ml−1) may cause a reduction in cheese yield or the development of off-flavours during ripening. Although some varieties continue to be made using raw milk, the milk for most cheeses is now pasteurized, causing changes to the microflora of the milk and to its complement of indigenous enzymes which can influence ripening. It is well known that cheese made from raw milk ripens more quickly and develops a stronger flavour than cheese of the same variety made from pasteurized milk (Fox et al., 1998) and these differences have been ascribed mainly to heat-induced changes to the native microflora of the milk. In addition to all potential pathogens, many organisms that otherwise would grow later to form part of the non-starter microflora are killed by pasteurization, and the biodiversity of cheese made from pasteurized milk is simpler than that made from raw milk (see Chapter 6). Although heat-induced changes to the microflora of the milk are mainly responsible for differences between raw and pasteurized milk cheese, inactivation of certain indigenous enzymes in milk, particularly lipoprotein lipase, may contribute also (see Collins et al., 2004). In commercial practice, the ratio of casein to fat, or increasingly their concentrations, is controlled by standardization which enhances the cheesemaking properties of the milk and improves cheese yield. Directly or indirectly, standardization influences some important compositional parameters of the final cheese which affect ripening (e.g., moisture and moisture-in-non-fat-substances).
Cheese is a fermented dairy product and, hence, the controlled fermentation of lactose to lactate by the starter during manufacture and the early stages of ripening is important in all varieties. The science and technology of cheese starter cultures have become very complex (see Parente and Cogan, 2004) and starter cultures play a major role in cheese ripening, directly through their many enzymes and indirectly through acidification and reduction of the redox potential. Since lactic acid bacteria (LAB) are auxotrophic for many amino acids, they possess a complex system of proteinases and peptidases that enable them to liberate amino acids from the caseins as they grow in milk. In cheese, the role of starter proteinases and peptidases appears to be principally in the degradation of intermediate-sized peptides and the liberation of free amino acids (see below). LAB also contain intracellular metabolic enzymes which catalyse the catabolism of amino acids and contribute directly to the formation of volatile flavour compounds (see Yvon and Rijnen, 2001; Collins et al., 2004; Curtin and McSweeney, 2004 and Chapter 4). The reduction in pH caused by the metabolism of lactose to lactate has a major indirect effect on ripening, through changes to (1) the retention of coagulant activity in the curd, (2) the rate of syneresis and hence the final level of moisture in the curd, (3) control of the growth of added and native microorganisms in the cheese, and (4) the activity of enzymes involved in ripening.
The milk for rennet-coagulated cheese varieties is coagulated via limited proteolysis of κ-casein at or near Phe105–Met106, through the action of selected proteinases in rennet preparations, followed by the Ca²+-induced aggregation of rennet-altered micelles at a temperature greater than ~18°C (Horne and Banks, 2004). The traditional rennet used for the manufacture of most cheese varieties is a brine extract of the abomasa of milk-fed calves (or the young of other dairy animals), and contains principally chymosin with a low level of pepsin. However, alternatives to traditional calf rennet are now used widely, including fermentation-produced chymosin or enzymes from Rhizomucor miehei, Rhizomucor pusillus or Cryphonectria parasitica. Depending on factors such as enzyme type, pH at whey drainage, cook temperature and the moisture content of the curd, from ~0 to 15% of the rennet activity added to the milk is retained in the curd (Upadhyay et al., 2004) and, as discussed below, is a major proteolytic agent in the ripening of most varieties, catalysing mainly the hydrolysis of αs1-casein.
The gel formed on the rennet-induced coagulation of milk is quite stable if left undisturbed, but if it is cut or broken, it synereses rapidly, expelling the liquid entrapped within the gel as whey. The rate and extent of syneresis, and thus the moisture content of the cheese, are controlled during manufacture by varying factors such as the composition of the milk, size of curd particles, cooking temperature, rate of acidification, rate of stirring of the curds–whey mixture, and time (Fox and McSweeney, 2004). Operations at this stage of manufacture largely control the moisture content of the cheese and have a major indirect effect on ripening since, all else being equal, high-moisture cheeses will ripen more quickly than cheeses with a low moisture content. A high cooking temperature (e.g., during the manufacture of Swiss-type cheeses or Italian Grana-type varieties) also influences ripening since, in addition to promoting syneresis, it inactivates much of the remaining chymosin, while the level of plasmin, a heat-stable enzyme, is increased through the denaturation of plasmin inhibitors and the inhibitors of plasminogen activators (Farkye and Fox, 1990).
The curds for Cheddar and related varieties are texturized after whey drainage. During this ‘cheddaring’ process, the pH of the curds decreases to ∼5.4, which causes dissolution of some colloidal calcium phosphate, thus altering the Ca:protein ratio and modifying the texture of the curd. In traditional practice, cheddaring is performed by the repeated piling and re-piling of curd blocks in the vat. However, this traditional practice serves simply to facilitate removal of a small amount of whey, to keep the curds warm and to allow time for acid to develop, and it has been replaced in industry by towers and belt systems which achieve the same result (see Bennett and Johnston, 2004). The curds for pasta-filata cheese (e.g., Mozzarella) are also allowed to develop acid and, after acidification, are heated to 60–65°C in hot water and stretched, which contributes to the desirable functional characteristics of melted Mozzarella used extensively as a pizza topping. The cooking–stretching step of pasta-filata cheeses also has a major influence on their ripening through the inactivation of much rennet activity and the killing of the starter bacteria (Kindstedt et al., 2004).
All cheeses are salted either by immersion in brine (most varieties), or by mixing dry salt with milled curd (Cheddar and related cheeses), or by application of dry salt to the surface of the cheese after moulding. The amount of salt added to cheese is characteristic of the variety; a low level of salt is added to Swiss-type cheeses while varieties ripened under brine (e.g., Feta) contain a high level of NaCl. The rate at which salt-in-moisture (S/M) increases is quite slow in brine-salted varieties, since NaCl must diffuse from the surface of the cheese, while uptake is very rapid in dry-salted varieties (e.g., Cheddar) where NaCl is mixed with milled curd (Guinee and Fox, 2004). The level of S/M and the rate at which S/M increases are factors that have a major influence on ripening (see Guinee and Fox, 2004). NaCl at >1.5% (w/w) inhibits acid production by the starter culture and thus, in some varieties (e.g., Cheddar which is dry salted), salt stops acidification and fixes the pH of the cheese for the early stages of ripening. In Swiss-type cheese, the growth of Propionibacterium freudenreichii is inhibited by NaCl to an extent determined by strain and pH. The growth of the secondary culture Penicillium roqueforti in Blue cheese is stimulated by 1% (w/w) NaCl but inhibited by >3–5% (w/w) NaCl, depending on the strain. Likewise, a low level of NaCl stimulates the growth of Penicillium camemberti on white-mould cheeses (see Guinee and Fox, 2004). NaCl also affects ripening through changes in the activity of enzymes. Plasmin, the principal indigenous proteinase in milk, is stimulated by 2% (w/w) NaCl but is inhibited by a high salt concentration (Noomen, 1978).
There is relatively little evidence for a direct effect of salt on microbial enzymes, although most are probably inhibited by moderately high NaCl levels, particularly at low pH (see Guinee and Fox, 2004). At concentrations typically found in cheese, NaCl probably has little direct effect on chymosin action during ripening. However, salt plays a major indirect role on the hydrolysis of the caseins by chymosin during ripening through its effects on its substrates. The hydrolysis of αs1-casein in dilute solution by chymosin is stimulated by NaCl to an optimum at ∼6% (w/w) (Fox and Walley, 1971) but its hydrolysis is retarded by very low levels of salt in cheese (see Guinee and Fox, 2004). Of more significance to cheese quality is the effect of NaCl on the hydrolysis of β-casein. Increasing the ionic strength of cheese through the addition of NaCl promotes interactions between the hydrophobic C-terminal regions of β-casein and inhibits the access of chymosin to its cleavage sites. Decreasing NaCl levels in the cheese facilitates chymosin action on β-casein and thus the production of hydrophobic peptides from the C-terminal of β-casein (e.g., β-CN f193-209) which are extremely bitter (Kelly et al., 1996). In addition to its indirect effects on flavour through its effects on microbial growth and enzyme activity, salt also has direct effects by contributing to the savoury flavour of cheese. Salt has a major effect on the composition of cheese, since ∼2 kg H2O are lost per kg NaCl absorbed (Fox et al., 2000), and thus also influences flavour and textural changes during ripening through its effect on water activity (aw) and the moisture content of cheese.
The final or penultimate step in the manufacture of curd is moulding and, in the case of low-moisture varieties, pressing. The curds for brine-salted cheeses are moulded prior to salting, while those for dry-salted varieties are moulded and pressed after the addition of salt. The size and shape into which the curds for a particular variety are moulded are often not simply cosmetic. For example, the traditional size and shape for Emmental is a large wheel up to 1m in diameter and weighing up to ∼100 kg. This large size is necessary to trap some CO2 produced during ripening and to allow it to reach a sufficient partial pressure to form eyes. Also, many surface-ripened varieties (e.g., Camembert or smear-ripened cheeses) are moulded into the form of a small, short cylinder. Since many important events during ripening occur at the surface, the ratio of surface area to volume is very important for these cheeses. If this ratio is too low (i.e., if the cheese is large), the surface may ripen excessively but the core may remain unripe.
1.2 Overview of cheese ripening
Rennet-coagulated cheeses are ripened for a period ranging from about two weeks (e.g., Mozzarella) to two or more years (e.g., Parmigiano-Reggiano or extra-mature Cheddar) to allow the flavour and texture characteristic of the variety to develop. During this time, major microbiological and biochemical changes occur in cheese.
Microorganisms gain entry into cheese curd either by deliberate addition as part of the starter culture, as added adjunct starters, or by being naturally present in the ingredients of cheese, particularly the milk. The composition of the cheese microflora is affected by the type of starter and adjunct used, pasteurization of the milk and the cooking temperature used during manufacture and, later, the environment of the cheese (i.e., NaCl and moisture levels, pH, presence of organic acids and nitrate, redox potential and temperature) (Beresford et al., 2001). Cheese ripening is characterized by a number of microbial changes. In most varieties, the starter reaches cell numbers of ≥10⁸ cfu g−1 within one day of manufacture, after which they die off, lyse and release their intracellular enzymes into the matrix of the curd (see Beresford and Williams, 2004; Lortal and Chapot-Chartier, 2005). However, some evidence is emerging which demonstrates that the starter culture only partially lyses, but rather remains unculturable yet metabolically active for production of flavour compounds (Stuart et al., 1998; Chou and Weimer, 2001; Ganesan et al., 2004a, b; Ganesan and Weimer, 2004). Non-starter lactic acid bacteria (NSLAB) are adventitious microorganisms, principally facultatively heterofermentative lactobacilli such as Lactobacillus casei and Lactobacillus paracasei. NSLAB grow in probably all ripened cheeses at a rate largely dependent on temperature, from a very low initial number (typically <10²cfu g−1 after manufacture) to ∼10⁷cfu g−1, thus often becoming the dominant viable microorganisms in many cheese varieties later in ripening, and they play a role in ripening (see Fox et al., 1998; Beresford and Williams, 2004).
The ripening of certain varieties is characterized by the growth of a secondary microflora that often dominates the ripening of these cheeses. Propioni-bacterium freudenreichii grow during the ripening of Swiss-type cheeses and are essential for the characteristic eye development (see Fröhlich-Wyder and Bachmann, 2004). After the manufacture of surface mould-ripened cheeses, yeasts including Kluyveromyces lactis, Saccharomyces cerevisiae and Debaryo-myces hansenii grow initially, together with the mould Geotrichum candidum. After 6 or 7 days of ripening, Penicillium camemberti begins to grow and forms the dense white felt characteristic of the surface of Camembert and Brie. Later during the ripening of these cheeses, Gram-positive coryneform bacteria begin to develop (Spinnler and Gripon, 2004). Yeasts also grow in Blue cheeses but the organism which dominates the ripening of these cheeses is the mould Penicillium roqueforti (Cantor et al., 2004). Finally, in bacterial surface-ripened, or smear-ripened, varieties yeasts grow initially on the surface and are followed by a very complex Gram-positive bacterial microflora composed of coryneform bacteria (Arthrobacter, Brachybacterium, Brevibacterium, Corynebacterium and Microbacterium spp.), micrococci and staphylococci (Brennan et al., 2004). This complex bacterial microflora gives these cheeses their characteristic red-orange colour and pungent aroma.
The biochemical changes which occur in cheese during ripening are often grouped into three major categories:
• Metabolism of residual lactose and of lactate and citrate
• Liberation of fatty acids from triacylglycerols (lipolysis) and the subsequent metabolism of fatty acids to various volatile flavour compounds
• Degradation of the casein matrix of the curd to a range of peptides and, ultimately, to free amino acids (FAA). FAA then act as substrates for a complex series of catabolic reactions which produce many important flavour compounds, especially carboxylic acids and sulfur compounds.
Since cheese is a fermented dairy product, the metabolism of lactose to lactate by the starter LAB is an essential feature of its manufacture. Most of the lactose in milk is lost in the whey as lactose or lactate but cheese curd at the start of ripening contains a low level of lactose. It is important that the residual lactose in cheese curd is completely metabolized to avoid the development of an atypical secondary flora or excessive Maillard browning on heating. The rate of metabolism of residual lactose in cheese early in ripening is determined largely by the S/M level in the curd, since this parameter greatly affects the action of starter bacteria. In Cheddar and related dry-salted varieties, starter activity is stopped very quickly at the end of manufacture, since the S/M level increases rapidly. In large brine-salted cheeses, the S/M level increases slowly as salt diffuses through the cheese. Lactose that remains unfermented by the starter bacteria is probably metabolized by the NSLAB flora (McSweeney and Fox, 2004). Lactose fermentation during the manufacture and the early stages of the ripening of Swiss-type cheeses is complex. The glucose moiety of lactose is metabolized quickly by Streptococcus thermophilus as the curd cools and galactose accumulates initially, but this sugar and any remaining lactose are metabolized by the thermophilic Lactobacillus present as a component of the starter culture (Turner et al., 1983; Fox et al., 1990).
Lactate is an important substrate for a series of reactions during ripening. In most cheeses, L-lactate is racemized slowly to DL-lactate by the action of the NSLAB flora. Racemization of lactate is not important for the flavour of cheese but it favours the development of Ca-lactate crystals (see McSweeney and Fox, 2004) which develop in cheese during ripening and, although harmless, may cause consumers to reject the cheese as containing foreign bodies or mould. Racemization appears to be important for the formation of Ca-lactate crystals as it lowers the concentration threshold for crystallization; however, racemization is not an absolute requirement for the development of Ca-lactate crystals.
Lactate can be metabolized by some LAB to acetate, ethanol, formate and CO2 (Fox et al., 2000) or by pediococci (occasionally present in cheese as a component of the NSLAB flora) to acetate and CO2 (Thomas et al., 1985). However, these pathways are not significant in cheese, particularly varieties ripened in film wrappings, due to the very low level of oxygen in the curd (McSweeney, 2004). A serious defect known as late gas blowing is caused by the anaerobic fermentation of lactate to butyrate and H2 and CO2 by Clostridium tyrobutyricum. Late gas blowing is of particular concern in brine-salted cheeses since the S/M level increases slowly; the defect may be avoided by strategies aimed at minimizing the numbers of spores in milk, physically removing the spores or preventing spore germination (see McSweeney and Fox, 2004).
Lactate metabolism is vital for the ripening of Swiss-type and surface mould-ripened cheeses (e.g., Camembert). In the former group of cheeses, lactate is metabolized by Propionibacterium freudenreichii by one of three pathways (Fig. 1.2), although the Wood–Werkman pathway is of minor importance. Strains of P. freudenreichii differ in their aspartase activity and hence in their ability to couple the fermentation of lactate with aspartate; strains with low aspartase activity metabolize lactate mainly by the classical propionate fermentation (Fröhlich-Wyder and Bachmann, 2004). The volatile carboxylic acids produced in these biochemical pathways contribute to the flavour of Swiss-type cheeses, while the CO2 migrates through the curd where some accumulates to form the eyes characteristic of these varieties.
Fig. 1.2 Utilization of lactate by Propionibacterium freudenreichii (after Fröhlich-Wyder and Bachmann, 2004).
The catabolism of lactate is extensive in surface mould-ripened cheeses (e.g., Camembert and Brie) where it is metabolized oxidatively at the cheese surface by Penicillium camemberti. Metabolism of lactate causes deacidification of the cheese surface, resulting in a pH gradient from the core into the exterior. When lactate is exhausted, Penicillium camemberti metabolizes proteins, ultimately producing NH3 that diffuses into the cheese. The concentration of calcium phosphate at the exterior exceeds its solubility at the high pH and it precipitates as Ca3(PO4)2 at the surface, thus causing the migration of calcium phosphate from the centre of the cheese towards its surface (Fig. 1.3). The movement of calcium phosphate from the centre of the cheese and the high pH lead to the characteristic softening of Camembert-type cheeses which become almost liquid on extended storage (McSweeney and Fox, 2004).
Fig. 1.3 Schematic representation of the changes which occur in Camembert-type cheese during ripening as a consequence of the growth of Penicillium camemberti at the cheese surface. (modified from McSweeney and Fox, 2004, with permission)
Although milk contains a relatively low level of citrate (∼8 mmol L−1) and most of it is lost in the whey, citrate is an important precursor for flavour compounds and CO2 which causes development of the few characteristic eyes in Dutch cheeses (Fox et al., 1990; Parente and Cogan, 2004; McSweeney and Fox, 2004). In Dutch-type cheeses, citrate is metabolized with the production of diacetyl, acetoin, 2,3-butanediol and CO2 by citrate-positive strains of Lacto-coccus, Leuconostoc mesenteroides subsp. cremoris or Leuconostoc lactis, although citrate may also be metabolized by some facultatively hetero-fermentative lactobacilli that are common components of the NSLAB flora.
As discussed in detail in Chapter 5 and by McSweeney and Sousa (2000) and Collins et al. (2003a, 2004), fat is an important source of many volatile flavour compounds in cheese. Unlike many high fat foods, lipid oxidation does not usually occur in cheese to an appreciable extent due to its low oxidation-reduction potential. However, triacylglycerols in cheese are hydrolysed by indigenous, endogenous and/or exogenous lipases to a range of fatty acids. Lipolytic enzymes in cheese generally originate from the milk, from the rennet preparation (if rennet paste is used) or to a limited extent from the cheese microflora. The indigenous lipoprotein lipase in milk is of most importance for lipolysis in raw milk cheeses, since this enzyme is extensively inactivated by pasteurization. Rennet extract used to coagulate milk for the manufacture of most cheese varieties is free from lipase activity. However, the milk for certain, mainly Italian and Greek, cheese varieties is coagulated using a rennet paste produced by macerating the stomach of the young dairy animal together with its contents. Rennet paste contains a potent lipase, pregastric esterase, which causes extensive lipolysis in cheeses such as the various Italian Pecorino varieties, Provolone and traditional Greek Feta.
The level of lipolysis in cheese which develops a secondary flora is usually related to the lipolytic activity of that flora. The complex Gram-positive bacterial flora which develops at the surface of smear-ripened varieties includes some organisms which are quite lipolytic and contribute to the liberation of fatty acids in these varieties. Propionibacterium freudenreichii is more lipolytic than LAB and contributes to lipolysis in Swiss cheeses during ripening. However, the most lipolytic secondary organisms associated with cheese are Penicillium spp. that grow in or on mould-ripened varieties. Penicillium roqueforti, enzymes from which catalyse the extensive lipolysis in Blue cheese, is very lipolytic; this organism produces two potent extracellular lipases with pH optima of 7.5–8 and 9–9.5. Penicillium camemberti, the characteristic mould growing on Camembert and Brie-type cheeses, produces one extracellular lipase that is optimally active at pH 9 and 35° C (Lamberet and Lenoir, 1976). A low level of lipolysis occurs in internal bacterially-ripened varieties made from pasteurized milk (e.g., Cheddar and Gouda) as a result of the action of enzymes from starter and non-starter LAB which, although weakly lipolytic, are present at high numbers for long periods of time (McSweeney, 2004). Lipolytic enzymes in LAB are intracellular and a relationship between cell lysis and lipolysis has been demonstrated in Cheddar cheese (Collins et al., 2003b).
Ruminant milk fat is rich in short chain fatty acids which, when liberated by lipolysis, contribute directly to the flavour of cheese. Although some lipolysis occurs in all cheeses, it is most extensive in varieties made using rennet paste, cheeses that are ripened for a long period of time or which develop a strongly lipolytic secondary flora (e.g., Blue or smear cheeses). Low levels of free fatty acids develop during the ripening of most other varieties (e.g., Swiss, Gouda); in these cheeses, excessive lipolysis is undesirable and results in rancidity (Collins et al., 2003a).
In addition to their direct contribution to cheese flavour, fatty acids serve as important precursors for many volatile flavour compounds produced through a series of pathways known collectively as fatty acid metabolism (Collins et al., 2003a, 2004; McSweeney, 2004). It was thought that esters were formed by direct reaction of an alcohol (usually ethanol) with a fatty acid. However, recent work (Liu et al., 2003; Holland et al., 2005) has provided evidence that the major pathway for the production of esters may be via a transferase reaction (alcoholysis; R1–COO–R2 + R3–OH → R1–COO–R3 + R2–OH). Thioesters are formed by the reaction of a fatty acid with a thiol compound, most commonly CH3SH, thus producing a range of S-methylthioesters (McSweeney and Sousa, 2000; Collins et al., 2003a, 2004). Fatty acid lactones are cyclic compounds formed through the intramolecular esterification of a hydroxyacid; both γ- and δ-lactones have been found in cheese and have five- and six-sided heterocyclic rings, respectively. Recent work by Alewijn et al. (2007) has suggested that lactones in Gouda cheese are formed by a one-step non-enzymatic reaction in which a hydroxy fatty acid esterified in a triacylglycerol undergoes an intra molecular transesterification to release a lactone directly. However, the metabolism of free fatty acids is most extensive and of most importance in Blue cheeses where fatty acids are metabolized to alkan-2-ones (n-methyl ketones; R–CO-CH3) by Penicillium roqueforti via a pathway similar to the early stage of β-oxidation. Approximately 11 alkan-2-ones have been found in cheese, but the most common are pentan-2-one, heptan-2-one and nonan-2-one which give the characteristic pungent aroma to Blue cheese (McSweeney, 2004). Alkan-2-ones may be reduced to their corresponding secondary alcohol (R–COH–CH3).
Proteolysis is perhaps the most complex biochemical event that occurs in most cheese varieties during ripening and the literature on this topic has been reviewed extensively (Grappin et al., 1985; Rank et al., 1985; Fox, 1989; Fox and Law, 1991; Fox et al., 1993, 1994, 1995a, b, 1996a; Fox and McSweeney, 1996, 1997; Sousa et al., 2001; Upadhyay et al., 2004). Proteinases and peptidases which catalyse proteolysis in cheese originate from six sources: the milk, the coagulant, starter LAB, NSLAB, secondary cultures and, in rare cases, exogenous proteinases (e.g., used to accelerate ripening).
Enzymes from the coagulant (usually chymosin) play a very important role in ripening, acting principally on αs1-casein which is cleaved at a number of sites, forming peptides including αs1-CN (f1-23), (f24-199) and (f102-199). As discussed above, chymosin action on β-casein in cheese is strongly inhibited by the presence of NaCl. αs2-Casein and para-κ-casein appear to be relatively resistant to chymosin action in cheese, although the former protein may be hydrolysed slowly by chymosin in vitro.
The role of the indigenous milk proteinases in cheese ripening has been the subject of extensive study (see reviews by Kelly and McSweeney, 2003; Upadhyay et al., 2004). The principal proteinase in milk, plasmin, is produced from its inactive precursor, plasminogen, under the control of a complex system of activators and inhibitors. Plasmin acts principally on β-casein during ripening, producing γ1-, γ2- and γ3-caseins and proteose peptones. In vitro, αs2-casein is a very good substrate for plasmin and this protein disappears in many cheeses during ripening. Although this phenomenon has not been studied in detail, it is likely that plasmin degrades αs2-casein during ripening. Recently, the role of lysosomal proteinases from somatic cells in cheese ripening has been studied (see Hurley et al., 2000a; Kelly and McSweeney, 2003; Upadhyay et al., 2004). The presence in milk of cathepsins D and B has been confirmed and a role for the former in cheese ripening has been demonstrated, at least under certain circumstances (Hurley et al., 2000b).
Although a portion of the starter culture lyses during ripening, their enzymes, most of which are intracellular, contribute to flavour production via increased access to substrate; intact cells may also remain metabolically active (Ganesan et al., 2006; Stuart et al., 1998). The principal proteinase of most LAB is lactocepin, a serine proteinase loosely attached to the cell surface and the gene for which is plasmid-encoded. When the cell is growing in milk, lactocepin acts to degrade caseins; however, the major role of this enzyme in cheese ripening appears to be in the degradation of intermediate-sized peptides produced from the caseins by plasmin or chymosin (Upadhyay et al., 2004). Lactococci, and perhaps other genera of LAB, also possess intracellular proteinases, although their role in cheese ripening is unclear. LAB possess a wide range of intracellular peptidases (Fig. 1.4), including oligoendopeptidases, di- and tripeptidases, aminopeptidases and a number of proline-specific peptidases but apparently no carboxypeptidase. Proline-specific peptidases are of particular importance since the caseins are rich in this amino acid and, due to its ring structure, many peptidases are unable to hydrolyse proline-containing peptides. Peptidases of LAB act on short peptides, often releasing free amino acids. The extensive literature on the peptidases of LAB was summarized recently by Upadhyay et al. (2004).
Fig. 1.4 Proteolytic enzymes of Lactococcus that contribute to cheese ripening (from Parente and Cogan, 2004, with permission).
The proteinase/peptidase systems of NSLAB appear to be generally similar to those of starter LAB and the proteolytic systems of secondary organisms in cheese often play significant roles in ripening. Penicillium camemberti and Penicillium roqueforti synthesize aspartyl- and metalloproteinases and an acid carboxypeptidase (Gripon, 1993). Geotrichum candidum also produces extracellular and intracellular proteinases but it is thought that its contribution to proteolysis in Camembert is less than that of Penicillium camemberti (Gripon, 1993). As discussed above, smear-ripened cheeses are characterized by the growth of a complex Gram-positive bacterial flora. Although organisms from a number of genera are present on the surface of these cheeses, enzymes from Brevibacterium linens have been studied in most detail, although some information is available about enzymes from Arthrobacter nicotianae and Micrococcus spp. Brevibacterium linens secretes extracellular proteinases, extracellular aminopeptidases and intracellular proteinases and peptidases (see Rattray and Fox, 1999; Upadhyay et al., 2004). The secondary organism of Swiss-type cheeses, Propionibacterium freudenreichii, is weakly proteolytic but does produce active peptidases which contribute to the ripening of these varieties (Gagnaire et al., 1999).
Proteolysis contributes to the development of cheese texture directly through hydrolysis of the casein matrix of cheese and by reducing the aw of cheese through changes to water binding by the COO− and NH3+ groups liberated on hydrolysis of a peptide bond and, indirectly, via an increase in pH caused by the liberation of NH3 from amino acids produced by proteolysis. Proteolysis also contributes to the flavour and off-flavour of cheese by producing short peptides and amino acids, some of which have flavours, and by facilitating the release of sapid compounds from the cheese matrix during mastication (Upadhyay et al., 2004). However, in recent years, it has become apparent that the most important role of proteolysis in the biogenesis of cheese flavour is through the production of free amino acids which are catabolized to a wide range of volatile flavour compounds. Amino acid catabolism has been an active area of research in recent years and the topic has been reviewed (McSweeney and Sousa, 2000; Yvon and Rijnen, 2001; Smit et al., 2002; Curtin and McSweeney, 2004; Ardö, 2006) and is discussed in detail in Chapter 4.
Amino acids in cheese appear to be catabolized by two major pathways (Yvon and Rijnen, 2001) initiated by the action of an aminotransferase or an amino acid lyase. Other pathways including decarboxylation and deamination also occur; the latter may be quite important in certain varieties (e.g., Gruyère) in which much NH3 is produced during ripening. The details of catabolic pathways remain to be elucidated fully, and work to date has concentrated on branched-chain and aromatic amino acids and methionine. These investigations have provided insight into the production of many flavour compounds in cheese. As an example, the catabolic pathways for leucine are shown in Fig. 1.5.
Fig. 1.5 Pathways for the catabolism of leucine; similar catabolic pathways also exist for the other branched-chain amino acids (from McSweeney, 2004, with permission).
1.3 Bitterness
Bitterness is a taste sensation perceived towards the back of the tongue and is a taste defect associated with dairy products including cheese, fermented milks and casein hydrolysates. Literature on the bitter defect was reviewed by Lemieux and Simard (1991, 1992), McSweeney (1997) and McSweeney et al. (1997). Although numerous compounds in cheese have a bitter taste at sufficient concentration, the bitter defect in cheese results from the excessive accumulation of hydrophobic peptides. The mean hydrophobicity (Q) of a peptide is an important factor in determining the bitterness of a peptide (McSweeney, 1997):
where Δft is the hydrophobicity of the amino acid side chain (free energy of transfer) and n is the number of amino acid residues in the peptide. However, the distribution of hydrophobic amino acid residues along the peptide chain also influences bitterness (Adler-Nissen, 1986). Therefore, degradation of proteins with a high mean hydrophobicity is likely to produce bitter peptides; this is of particular significance for cheese as the caseins are relatively hydrophobic proteins. Peptides of molecular mass ca. 0.1 to 6kDa with Q > 1400 cal residue−1 are often bitter. Thus, bitterness is principally associated with short, hydrophobic peptides; larger peptides, even if they are relatively hydrophobic, are perceived as being less bitter than a short peptide of the same value of Q. Likewise, the degradation of a short peptide into its constituent amino acids residues through the action of exopeptidases reduces the intensity of bitterness.
The bitter defect in cheese occurs when hydrophobic short peptides accumulate to an excessive extent either due to overproduction or to inadequate degradation due to lack of peptidase activity. Certain starter strains are associated with the development of bitterness either because their proteinases (particularly lactocepin) produce bitter peptides directly from precursor polypeptides or, more likely, because they lack sufficient peptidase activity necessary to degrade bitter peptides produced by other enzymes (e.g., chymosin).
The specificity of different proteinases on a given protein substrate is also of significance to the development of bitterness. Plasmin, which cleaves β-casein towards its N-terminus and at the centre of the molecule, produces much less bitterness than chymosin which cleaves at the very hydrophobic C-terminal region of this protein and can produce very bitter peptides (e.g., β-CN f193-209) directly. Indeed, the action of chymosin is of great significance to the development of bitterness. Hence, factors which influence the retention of rennet activity in the curd (e.g., type and quantity of rennet used, drain pH, cooking temperature) can influence the development of bitterness.
The pH of cheese also influences the development of bitterness by affecting the activity of chymosin and other enzymes. The level of salt in cheese has a major role in the development of bitterness, since NaCl concentration is a major factor influencing the ionic strength (μ) of the aqueous phase of cheese. The development of bitterness in cheese is dependent on ionic strength, since a high μ favours the hydrophobic association of the C-terminal region of β-casein and perhaps other large, hydrophobic but non-bitter polypeptides, thus inhibiting chymosin action (Fox and Walley, 1971). Hence, cheese with a low salt content is very prone to bitterness (Stadhouders and Hup, 1975; Stadhouders et al., 1983; Visser et al., 1983; Kelly et al., 1996). NaCl also inhibits lactocepin (Exterkate, 1990) and the affects the porosity of the starter cell wall (and thus the release of intracellular peptidases; Visser et al., 1983).
The use of exogenous proteinases (e.g., to accelerate ripening: see Fox 1988/89, or in the manufacture of enzyme-modified cheese, see Kilcawley et al.,1998) often causes the development of bitterness, as does the use of coagulants with an excessive ratio of general proteolysis to milk coagulating activity (e.g., certain plant enzymes). Bitterness is also often encountered during the ripening of reduced fat cheese (Banks et al., 1992), perhaps due to reduced opportunity for hydrophobic peptides to partition into the lipid phase. Cheese made from milk containing high levels of proteinases produced by psychrotrophic bacteria may also develop bitterness (Hicks et al., 1986) or factors that reduce starter culture numbers (e.g., bacteriophage or antibiotics) and thus reduce the level of LAB peptidases in the cheese matrix.
Bitterness is also of significance to casein hydrolysates and various strategies have been adopted to ameliorate this defect, including adsorption of hydrophobic peptides onto activated charcoal, their removal using hydrophobic interaction chromatography, solvent extraction or isoelectric precipitation, the use of cyclodextrins as masking agents or hydrolysis of bitter peptides using exopeptidases (see McSweeney et al., 1997). In cases where bitterness develops unavoidably in cheese, the most useful debittering strategy involves the use of starters, adjuncts or enzyme preparations with high exopeptidase activities. Koka and Weimer (2000) also found that bitter peptides found in Cheddar cheese could be hydrolysed by the purified proteinase of Pseudomonas fluorescens RO98.
1.4 Acceleration of cheese ripening
Cheese ripening is a slow, and thus expensive, process. Costs involved in cheese ripening stem primarily from the inventory cost of delaying the sale of a large proportion of a year’s production, the capital cost associated with ripening rooms and the need to control temperature and, often, relative humidity. The cost of ripening a hard cheese such as Cheddar has been estimated at approximately €500–800 (US$640–1025) per tonne of cheese matured for nine months (Upadhyay and McSweeney, 2003). Hence, methods to accelerate cheese ripening have received considerable attention in the scientific literature and have been reviewed by Fox (1988/89), El Soda and Pandian (1991), Wilkinson (1993), Fox et al. (1996b) and Upadhyay and McSweeney (2003). Various approaches used to accelerate cheese ripening include:
• Addition of exogenous enzymes
• Increasing the level of LAB enzymes through the use of attenuated starters or an increased rate of lysis
• Use of adjunct cultures
• Genetic modification of starter bacteria
• The use of high hydrostatic pressures
• Elevated ripening temperature.
The addition of free or encapsulated enzymes to cheese at various stages of manufacture has been studied by numerous authors but with limited success (see Upadhyay and McSweeney, 2003). Apart from the fact that much of the enzyme added to the milk may be lost in the whey, the addition of single enzymes will accelerate only one step in the complex series of biochemical events that constitutes cheese ripening, often leading to an unbalanced flavour. The use of a mixture of enzymes has the major advantage of accelerating multiple ripening steps and a number of such preparations, usually containing proteinases, peptidases and, often, lipases are available commercially (see Upadhyay and McSweeney, 2003).
Another approach to increase the enzyme complement in cheese is to add enzymes naturally encapsulated within attenuated cells (Klein and Lortal, 1999). Attenuated starters are LAB which are unable to produce acid during cheese manufacture but which can provide enzymes that contribute to ripening. LAB cells may be attenuated by heat-shock, freezing/thawing, freeze or spray drying, lysozyme treatment, use of solvents or through natural (e.g., by the removal of a plasmid to produce lactase-negative mutants) or induced genetic modification. The advantages of attenuated starters include that they contain a wide range of enzymes, are subject to few legal barriers and are largely retained in the cheese curd. Lysis of LAB cells occurs during ripening at a rate dependent on the strain and liberates many enzymes important for ripening into the matrix of the curd. Acceleration of lysis through the use of bacteriophage, bacteriocins or bacteriocin-producing cultures may influence ripening (see Upadhyay and McSweeney, 2003). However, the correct balance between intact and lysed cells is important for ripening, as the former may be metabolically active and can catalyse co-factor dependent reactions more easily (Crow et al., 1995).
The use of adjunct cultures to accelerate ripening or to modify cheese flavour has shown considerable promise. Adjunct starters are organisms which are added to cheesemilk or encouraged to grow in or on cheese but which do not contribute to acidification. Many cheeses are made using secondary cultures (e.g., Propionibacterium freudenreichii in Swiss-type cheeses, Penicillium camemberti or Penicillium roqueforti in mould-ripened cheeses, or a complex Gram-positive bacterial surface flora on smear-ripened cheeses). Indeed, Cheddar is amongst the few varieties which are not traditionally made using secondary cultures. Hence, much research has been focused on the effects of NSLAB and thermophilic lactobacilli as adjuncts on the ripening of full-fat and reduced-fat Cheddar and most success has been achieved with the latter adjuncts (e.g., Tobin, 1999; Hannon et al., 2003). Use of surface ripening cultures as adjuncts has also met with some success to accelerate ripening of reduced-fat Cheddar cheese (Weimer et al., 1997).
Despite substantial research and highly successful mutation strategies for genetic modification in LAB, approaches to accelerating cheese ripening involving genetic modification (GM) of starter bacteria have achieved little commercial success, mostly due to regulatory and consumer concerns related to the use of GM organisms in foods and partly because the enzymes targeted (mainly proteinases and peptidases) play a relatively minor direct role in the development of cheese flavour (see Upadhyay and McSweeney, 2003). However, recent research on amino acid catabolic enzymes (for reviews see Yvon and Rijnen, 2001; Curtin and McSweeney, 2004; Ardö, 2006) and other enzymes which are important for the production of volatile flavour compounds may give impetus to the construction of GM starters with improved cheesemaking potential. High hydrostatic pressures have been investigated as a means of accelerating ripening (see Trujillo et al., 2000; O’Reilly et al., 2001; Huppertz et al., 2002; Upadhyay and McSweeney, 2003). However, despite an early report of the usefulness of this technique (Yokoyama et al., 1992), recent research has shown only modest acceleration of ripening, probably as a consequence of increased lysis due to the pressure treatment (Upadhyay and McSweeney, 2003).
Probably the most efficient and simplest method for accelerating the ripening of hard cheeses is the use of an elevated ripening temperature. Increasing the ripening temperature accelerates proteolysis (e.g., Aston et al., 1983a, b; Fedrick et al., 1983; Folkertsma et al., 1996), lipolysis (Folkertsma et al., 1996; O’Mahony et al., 2006) and influences cheese microflora (Cromie et al., 1987; Folkertsma et al., 1996). However, elevated temperatures may cause texture defects during ripening (e.g., changes to the shape of the cheese or exudation of liquid fat at the surface). In addition, elevated temperatures may increase the risk of microbial spoilage or the development of an unbalanced or poor flavour, and hence cheese ripened at a high temperature should be monitored very closely. Nevertheless, it appears that a ripening temperature of up to ca. 15°C (Fedrick, 1987; Folkertsma et al., 1996) is a potentially viable approach to accelerate the ripening of Cheddar cheese made in large factories with good hygiene and adequate monitoring systems.
1.5 Acknowledgement
The author wishes to express his thanks to Prof. P.F. Fox for helpful comments on the manuscript of this chapter.
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