CyTA - Journal of Food

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Production, physico-chemical and functional

characterization of a protein isolate from jackfruit
(Artocarpus heterophyllus) seeds

Jos Armando Ulloa, Mayte Carolina Villalobos Barbosa, Juan Alberto

Resendiz Vazquez, Petra Rosas Ulloa, Jos Carmen Ramrez Ramrez, Yessica
Silva Carrillo & Liborio Gonzlez Torres

To cite this article: Jos Armando Ulloa, Mayte Carolina Villalobos Barbosa, Juan Alberto
Resendiz Vazquez, Petra Rosas Ulloa, Jos Carmen Ramrez Ramrez, Yessica Silva Carrillo &
Liborio Gonzlez Torres (2017): Production, physico-chemical and functional characterization of
a protein isolate from jackfruit (Artocarpus heterophyllus) seeds, CyTA - Journal of Food, DOI:
10.1080/19476337.2017.1301554

To link to this article: http://dx.doi.org/10.1080/19476337.2017.1301554

2017 The Author(s). Published by Informa Published online: 07 Apr 2017.

UK Limited, trading as Taylor & Francis
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CYTA JOURNAL OF FOOD, 2017
http://dx.doi.org/10.1080/19476337.2017.1301554

Production, physico-chemical and functional characterization of a protein isolate

from jackfruit (Artocarpus heterophyllus) seeds
Jos Armando Ulloaa,b, Mayte Carolina Villalobos Barbosab, Juan Alberto Resendiz Vazquezb, Petra Rosas Ulloaa,
Jos Carmen Ramrez Ramrezc, Yessica Silva Carrillod and Liborio Gonzlez Torrese
a
Centro de Tecnologa de Alimentos, Universidad Autnoma de Nayarit, Tepic, Nayarit, Mxico; bPosgrado de Ciencias Biolgico Agropecuarias,
Unidad Acadmica de Agricultura, Universidad Autnoma de Nayarit, Xalisco, Nayarit, Mxico; cUnidad Acadmica de Medicina Veterinaria y
Zootecnia, Universidad Autnoma de Nayarit, Compostela, Nayarit, Mxico; dUnidad Acadmica de Agricultura, Universidad Autnoma de
Nayarit, Xalisco, Nayarit, Mxico; erea de Ciencias Bsicas e Ingenieras, Universidad Autnoma de Nayarit, Tepic, Nayarit, Mxico

ABSTRACT ARTICLE HISTORY

Proteins from jackfruit seed defatted flour were fractionated, characterized and extracted using an Received 30 September
alkaline solution and isoelectric precipitation, which was followed by an ultrasound treatment, for 2016 Accepted 25 February
preparation and determination of the physicochemical and functional properties of a protein isolate. 2017
Glutelins were the dominant fraction, which are composed of 1520 kDa polypeptides. The protein KEYWORDS
content, water and oil absorption capacity and least gelation concentration of the jackfruit seed Jackfruit seed; protein
protein isolate were 952.1 g/kg (dry basis), 6.42 ml water/g protein and 6.07 ml oil/g protein and 9% isolate; physico-chemical
(at pH 6), respectively, whereas the greatest protein solubility, emulsifying activity, emulsion properties; functional
stability, foaming capacity and stability were 94.4%, 127%, 127%, 254% and 164%, respectively, properties
and depended on the pH; the predicted PER was 2.36. In light of the functional and nutritive
PALABRAS CLAVE
properties determined in this study, jackfruit seed protein isolate could be a novel protein source for Semillas de jaca; aislado
use in food systems. protenico; propiedades
fisicoqumicas; propiedades
funcionales
Produccin y caracterizacin fisico-qumica y functional de un aislado protenico
de semillas de jaca (Artocarpus heterophyllus)
RESUMEN
A partir de harina desengrasada de semilla de jaca se fraccionaron, caracterizaron y extrajeron las
protenas mediante solubilizacin alcalina y precipitacin isoelctrica. Las protenas extradas se
trataron con ultrasonido para la preparacin de un aislado protenico, al cual se le determinaron las
propiedades fisicoqumicas y funcionales. La fraccin mayoritaria de las protenas fue de glutelinas
(683,6 34,2 g/kg protena), las cuales estn compuestas por polipptidos de 15-20 kD. El contenido
de protena, la capacidad de absorcin de agua, la capacidad de absorcin de aceite y la
concentracin mnima de gelacin del aislado protenico fueron 952,1 g/kg (base seca), 6,42 ml
agua/g protena, 6,07 ml aceite/g protena y 9% (a pH 6), respectivamente, mientras que los valores
ms grandes de solubilidad de protena, actividad emulsificante, estabilidad de la emulsin, capa-
cidad espumante y estabilidad espumante fueron 94,4%, 127%, 127%, 254% y 164%, respectiva-
mente, los cuales dependieron del pH. El valor predicho de la relacin de eficiencia protenica del
aislado protenico fue 2,36. En vista de las propiedades funcionales y nutritivas determinadas en
este estudio, el aislado protenico de semilla de jaca podra ser una fuente nueva de protena para
uso en sistemas alimenticios y potencialmente adecuado para su aplicacin en panes, pasteles,
coberturas, crema batida, helados, postres, aderezos para ensalada, embutidos y productos crnicos.

Introduction included in this estimation). Additionally, food waste is

expected to increase to approximately 126 Mt by 2020 if
The world produces approximately 1600 million tons of solid
additional prevention policies or activities are not under-
waste per year. The generation and inappropriate manage-
taken (Mirabella, Castellani, Sala, 2014). However, many of
ment of this waste is considered to be one of the primary
these wastes have the potential to be reused in other pro-
environmental problems associated with the emission of
duction systems.
methane and carbon dioxide, the emission of odors from
Waste from the food industry, which has recently been
landfill sites and damage to surface water and air quality
considered for potential use in human food, is derived from
(Angulo et al., 2012).
the processing of various food groups, such as fruit and
Some estimates indicate that up to 42% of food waste is
vegetables, milk, meat, root crops and oilseeds (Ribeiro da
produced by households, 39% of waste occurs in the food
Silva et al., 2014). Of particular interest is the research
manufacturing industry, 14% occurs in the food sector
focused on the recovery of waste from fruit industrialization
(ready to eat food, catering and restaurants) and 5% is lost
in which waste may represent 1060% by weight of the fruit
along the distribution chain (agricultural food loss is not

CONTACT Jos Armando Ulloa arulloa5@gmail.com Centro de Tecnologa de Alimentos, Universidad Autnoma de Nayarit, Ciudad de la Cultura
Amado Nervo, CP 63155 Tepic, Nayarit, Mxico; Posgrado de Ciencias Biolgico Agropecuarias, Unidad Acadmica de Agricultura, Universidad Autnoma de
Nayarit, Carretera Tepic-Compostela Km 9, CP 63780 Xalisco, Nayarit, Mxico
2017 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use,
distribution, and reproduction in any medium, provided the original work is properly cited.
2 J. A. ULLOA ET AL.
(OShea, Arendt, & Gallagher, 2012). Waste from fruits pro-
duced during processing includes the peel, rind, seeds and
unusable pulp, which are generally not used and conse-
quently discarded. The primary components present in the
fruit waste are fiber, sugars, fat, proteins, pectins, organic
acids, antioxidants, phenols, vitamins, minerals, flavors and
other bioactive substances (Reis et al., 2012).
Conversely, jackfruit (Artocarpus heterophyllus L.) is a tree
belonging to the family Moraceae and is widely distributed
in tropical countries such as Brazil, Thailand, Indonesia, India,
the Philippines and Malaysia (Madruga et al., 2014). Due to
its spontaneous proliferation in warmer regions, jackfruit is
now cultivated throughout the tropical coast of Mexico with
the state of Nayarit being the main producer in the country.
Jackfruit is composed of several berries having yellow
pulp and brown seeds encased in a hard shell. Such fruits
are oblong-cylindric in shape and typically 3040 cm in
length but can sometimes be up to 90 cm long. The fruit
usually weighs 3.510 kg, although a weight of 25 kg has
been reported. The residues after processing of jackfruit can
constitute up to 70% of the total weight of the fruit. A
portion of such residues is the seeds, which may constitute
from 8% to 15% of the total weight of the fruit (Swami,
Thakor, Haldankar, & Kalse, 2012).
Jackfruit seeds are a good source of starch (22%) and
dietary fiber (3.19%). Additionally, jackfruit seed contains
lignans, isoflavones and saponins, which are all phytonutri-
ents that have health benefits that are wide-ranging from
anticancer to antihypertensive, antiaging, antioxidant and
antiulcer (Omale & Friday, 2010). Protein is another compo-
nent that is present in jackfruit seeds with a composition
that is 17.837% depending on the variety of jackfruit
(Swami et al., 2012).
Therefore, jackfruit seeds may serve as a potential source
of a protein isolate, and the characterization of properties
such as water/oil absorption, solubility, jellification, emulsify-
ing capacity, and foaming capacity is technologically impor-
tant because they determine the potential application of
protein isolate food ingredients (Bernardino-Nicanor et al.,
2014). To our knowledge, there are no scientific information
vailable on the preparation of protein isolate from jackfruit
seeds or its functional properties.
The objective of this study was to prepare a protein
isolate from jackfruit seeds and to characterize its physico-
chemical and functional properties.
Materials and methods
Chemical and materials
All chemicals were purchased from either Merck (Darmstadt,
Germany) or Sigma-Aldrich (St. Louis, MO, USA) if not stated
otherwise. The jackfruit seeds were provided by Mexican
Tropical Organics S. de R.L. de C.V. located at Carretera Los
Cocos-Aticama s/n San Blas, Nayarit (Mexico). The jackfruit
seeds were washed with tap water, sliced to 3 mm using a
domestic food processor (Moulinex, Grupo Seb Mexico, S.A.
de C.V., Mexico, D.F.), dried on a steel tray at 30C (Mod. 27,
Precision Scientific Group, Chicago, USA) for 8 h and then
pulverized in a mill (Cyclotec Mod. 1093, Foss Tecator,
Slangerupgade, Denmark). This jackfruit seed flour was
defatted using a Soxhlet extractor with ethylic ether for
16 h. The defatted flour was air-dried at room temperature.
Protein fractionation
Proteins were extracted from jackfruit seed defatted flour
based on their solubility according to the Osborne fractiona-
tion procedure as described by Amza, Amadou, Balla and
Zhou (2015). Total protein content of jackfruit seed defatted
flour protein fractions (albumin, globulin, glutelin and prola-
min) was measured using the Bradford method (1976) and
bovine serum albumin as standard.
Determination of molecular weight distribution
A study for determination of the molecular weight distri-
bution of the protein fractions from jackfruit seed defatted
flour was conducted according to the method reported by
Laemmli (1970). Sodium dodecyl sulfate-polyacrylamide
gel electrophoresis (SDS-PAGE) test was carried out
under reducing and nonreducing conditions using buffer
solution with and without 2-mercaptoethanol, respectively,
on a gel slab comprised 14% separating gel and 4%
stacking gel. Supernatant protein fractions (aliquots of
20 L in buffer [20 L] containing 65.8 mM TrisHCl,
26.3% glycerol, 2.1% SDS and 0.01% bromophenol blue)
were heated at 95C for 5 min. Aliquots (20 l) of the
prepared samples were loaded onto the gels. A wide-
range molecular weight marker 161-0317 (Bio-Rad
Hercules, USA) ranging from 6.5 to 200 kDa was used to
prepare a standard curve for molecular weight estimation.
The molecular weights of the samples were obtained by
Quantity One 1-D analysis software (Bio-Rad, Hercules,
CA, USA).
Preparation of the protein isolate
First, a study was conducted to determine the minimal and
maximal pH (in the range of 311) of protein extraction from
the defatted flour according to the method reported by
Bernardino-Nicanor et al. (2014). The defatted flour from
the jackfruit seeds was mixed with distilled water at a ratio
of 1:20 and adjusted to the pH of the maximal protein
extraction using 1.0 M NaOH. The slurry was stirred for
30 min at 25C and then centrifuged at 4500 rpm. The pH
of the supernatant was adjusted to the pH of the minimal
protein extraction (isoelectric point) with 1.0 M HCl, and the
slurry was stirred for 20 min at 25C. The precipitate was
separated by centrifugation at 4500 rpm for 20 min at 25C.
Then, the protein precipitate was subjected to an alcoholic
extraction with 96% ethanol, using a ratio of 1:10 (protein
precipitate:ethanol), stirred for 20 min, separated by centri-
fugation at 4500 rpm for 20 min at 25C and finally freeze
dried.
To estimate the effect of ultrasound on the protein con-
centration of the protein in the isolate previously obtained, a
suspension (ratio 1:10, protein isolate:water) of protein iso-
late was prepared and sonicated in an ultrasound bath
(Bransons Mod. 3510R-MT, 100 W42.5 kHz, Richmond, VA
23238) for 1 h. Subsequently, the protein isolate suspension
was treated according to the same procedure previously
applied to obtain the protein isolate from the defatted jack-
fruit seed flour, and this isolate will be hereinafter referred to
as the jackfruit seed protein isolate treated with ultrasound
(JPIU). This isolate was used for the physicochemical and
functional analyses.

Physicochemical analyses
Physicochemical characterization was determined using
proximate, bulk density and color analyses. For the prox-
imate analysis, moisture, crude protein (N 6.25), crude
fiber and ash contents were determined in triplicate
according to AOAC (1990) methods. The bulk density was
determined using the method described by Monteiro and
Prakash (1994). After a calibrated plastic centrifuge tube
had been weighed, it was filled with a protein sample up
to 25 ml and tapped to eliminate the spaces between
particles; the volume was then recorded as the volume
of the sample. After the tube had been weighed again,
the bulk density of the protein sample was calculated from
the difference in weight and expressed as g/ml. The color
was determined using a Minolta CR-400 color meter
(Minolta Ltd, Co., Tokyo, Japan). The measured values
were expressed according to the CIELAB color scale
where L* = lightness, +a* = redness, a = greenness,
+b* = yellowness and b = blueness. The L*, a* and b*
values of the white standard tile used as reference were
97.14, 0.19 and 1.84, respectively.
Amino acid analyses and protein quality
The hydrolysis and quantification of amino acids of protein
isolate from jackfruit seed defatted flour were performed
according to the methods reported by Erkan, Selcuk and
Ozden (2010), using a Waters high-performance liquid chro-
matographic system (Milford, MA, USA) consisting of a sys-
tem controller, auto injector, liquid chromatographic pump,
fluorescence detector and degasser. The different amino
acids recovered were presented as g/100 g protein isolate.
The protein quality of protein isolate was evaluated by mean
of the amino acid score and the predicted protein efficiency
ratio (PER) value.
The amino acid score was calculated by the following
equation:
g of amino acid per g test protein isolate
Amino acid score %  100
g of aminoacid per g standard pattern
where the standard pattern used was the Food and
Agriculture Organization of the United Nations/World
Health Organization (FAO/WHO, 1991) reference for adults.
The predicted PER was calculated from the amino acid
composition based on the equation developed by Alsmeyer,
Cuningham and Happich (1974), as given below.
PER 0:684 0:456Leu  0:047Pro
where Leu and Pro are the mass fractions of leucine and
tyrosine, respectively, expressed in g per 16 g of N.
Functional properties
The water absorption capacity was measured according to
the method outlined by Sosulski (1962). First, 0.5 g of protein
isolate was placed in a previously weighed 25-ml centrifuge
tube. Then, 10 ml of distilled water was added and the
mixture was stirred to homogeneity with a glass rod and
centrifuged at 3050 g for 10 min at room temperature (25
C). The supernatant was decanted, and the residue was
weighed together with the centrifuge tube. The water
absorption capacity was expressed as g water absorbed/g
CYTA JOURNAL OF FOOD 3
protein. A similar method was used to measure corn oil
absorption capacity; a 1-g sample was used for this purpose.
The emulsifying capacity was determined according to
the method outlined by Beuchat (1977). A 2-g sample of
protein isolate was blended with 100 ml of distilled water in
an Osterizer blender (Tlalnepantla, Edo. de Mexico) on high
speed for 30 s. Corn oil was gradually added from a grad-
uated burette while the mixture was being homogenized.
The decrease in consistency (from a maximum), which was
judged by a decrease in the resistance to blending, was
considered to be the point of oil addition discontinuation.
The amount of oil added up to this point was interpreted as
the emulsifying capacity of the sample. The result was
expressed as ml oil required to break the emulsion per g
protein.
To determine the protein solubility, samples of protein
isolate were suspended in water at different pH values (2
12) using the method described by Wang and Kinsella
(1976). These solutions were then centrifuged at 3050 g
for 10 min, and the supernatants were analyzed for protein
using the Kjeldahl method (AOAC, 1990).
The least gelation concentration was determined using
the method described by Abbey and Ibeh (1988). Protein
isolate samples were mixed with 5 ml of distilled water in
centrifuge tubes to obtain 2%, 4%, 6%, 8%, 10%, 12%, 14%,
16%, 18% and 20% concentrations; the pH of the suspen-
sions was adjusted to 2, 4, 6, 8 or 10 using 0.1 M HCl or
NaOH. The centrifuge tubes were heated for 1 h in a boiling
water bath, cooled rapidly under running tap water and
further cooled for 2 h in a refrigerator at 4C. The least
gelation concentration was considered to be the lowest
concentration at which the sample in the inverted tube did
not fall or slip.
A modified version of the method described by
Yasamatsu et al. (1972) was used to determine the emulsify-
ing activity (EA) and the emulsion stability of the isolate. Five
suspensions were prepared by dissolving 1 g of protein
isolate in 30 ml of water, and the pH of the suspensions
was adjusted to 2, 4, 6, 8 or 10 with 0.1 M HCl or NaOH.
Then, 30 ml of corn oil was added to each suspension. Each
mixture was stirred in an Osterizer blender at medium
speed for 1 min and centrifuged at 1190 g for 5 min. The
volume of the emulsion layer was recorded. The EA was
calculated as follows:
 
volume of emulsified layer
EA %  100
volume of total content in tube
Additionally, to determine the emulsion stability, the
samples were heated at 80C for 30 min in a water bath,
cooled to 25C in running water and centrifuged as above.
The emulsion stability was expressed as the percentage of
EA remaining after heating.
To determine the foaming properties, five suspensions
were prepared by dissolving 2 g of protein isolate in
100 ml of distilled water; the pH of the suspensions was
adjusted to 2, 4, 6, 8 or 10 using 0.1 M HCl or NaOH. The
suspensions were then whipped in an Osterizer blender at
low speed for 1 min at room temperature (25C). The
resulting foam was poured into a 250-ml cylinder. The total
foam volume was recorded, and foaming capacity was
expressed as the percentage increase in volume. The foam
stability (FS) was determined according to the method
4 J. A. ULLOA ET AL.
proposed by Kabirullah and Wills (1982). The foam volume
was recorded 30 min after whipping, and the FS was calcu-
lated as follows:
 
foam volume after 30 min
FS % 100
initial foam volume
Statistical analysis
Data from all experiments were collected in triplicate and
subjected to an analysis of variance and a multiple compar-
ison using Duncans test through the use of Statgraphics
Plus Version 4.0 (Manugistics, Inc., Rockville, MD, USA). The
level of significance was set at p < 0.05.
Results and discussion
Protein fractionation
The Osborne solubility-based protein fractionation data indi-
cated that NaOH-soluble (glutelin) and water-soluble (albu-
min) proteins were the predominant fractions in jackfruit
seed, 683.6 34.2 g/kg protein and 183.6 8.2 g/kg protein,
respectively, while, only 113.0 5.6 g/kg protein of NaCl-
soluble fraction (globulin) and 19.8 0.8 g/kg protein of
ethanol-soluble fraction (prolamin) was determined. Namely,
the vast majority of storage proteins in jackfruit seed were of
the glutelin and albumin form. This protein fraction distribu-
tion is similar to that found in other fruit seeds as seinat
(Cucumis melo var. tibish) seeds which comprises mostly
glutelins (386.5 g/kg), followed by albumins (345.3 g/kg),
globulins (240.7 g/kg) and prolamins (27.5 g/kg) (Siddeeg,
Xu, Jiang, & Xia, 2015), while that in the proteins of ginger-
bread plum seeds, the glutelin, albumin, globulin and prola-
min fractions were 406 g/kg protein, 276 g/kg protein,
258 g/kg protein and 64.8 g/kg protein, respectively (Amza
et al., 2015). Moreover, as determined in this study, the
glutelins was the main fraction of the protein extracted
Figure 1. SDS-PAGE profiles of protein fractions from jackfruit seed defatted flour in nonreducing (a) and reducing (b) conditions. Lane M, standard protein
markers with molecular weights of 6.5200 kDa; Lane 1, albumin fraction; Lane 2, globulin fraction; Lane 3, prolamin fraction; Lane 4, glutelin fraction.
Figura 1. Perfiles de SDS-PAGE de las fracciones protenicas de la harina desengrasada de semilla de jaca en condiciones no reductoras (a) y reductoras (b).
Lnea M, marcadores protenicos estndar con pesos moleculares entre 6,5200 kDa; Lnea 1, fraccin albmina; Lnea 2, fraccin globulina; Lnea 3, fraccin
prolamina; Lnea 4, fraccin glutelina.
from rice (Sing & Matta, 2008) and guava (Bernardino-
Nicanor, Scilingo, Aon, & Davila, 2006) seeds.
Distribution of molecular weight
SDSPAGE analysis results for the four protein fractions from
jackfruit seed defatted flour at nonreducing and reducing
conditions are shown in Figure 1. As observed in the non-
reducing patterns, the albumin and globulin fractions have
slightly different polypeptide composition profiles. The glu-
telin fraction appears as smears of two bands around the 20
and 15 kDa, in contrast with bands of high molecular mass
(higher than 94 kDa) observed in glutelins from guava seed
(Bernardino-Nicanor et al., 2006), while the globulin fraction
had six bands at 32, 29, 21, 19, 15 and 10 kDa with the 21
10-kDa in the highest proportion, in comparison with the
globulins from grape seed endosperm which showed many
bands in the 2565 kDa range, in particular, three major
polypeptides of about 35, 40 and 60 kDa, as well as an
approximately 8 kDa band (Gazzola et al., 2014). Moreover,
the albumin fraction had five bands at 32, 29, 23, 19 and
15 kDa, while the albumin from Akebia trifoliata var. australis
seed displayed eight distinct subunits with major bands at
about 49.0, 46.5, 35.6, 30.3, 19.0, 16.5, 13.9 and 12.3 kDa, but
the most concentrated bands were at 30.3 and 49.0 kDa (Du
et al., 2012). Under reducing conditions, albumin, globulin
and glutelin fractions had similar peptide compositions as
the nonreducing gel, which suggests minimal concentra-
tions on disulfide bonds in the proteins (Ajibola, Malomo,
Fagbemi, Rotimi, & Aluko, 2016). The albumin and globulin
fractions had six bands at 31, 27, 23, 20, 15 and 12 kDa. The
prolamin fraction was not detected in reducing and without
reducing conditions, suggesting that the protein in the
extraction fractions was not very soluble in the reagent
buffer and was possibly denatured by the organic solvent
used for their extraction, such as has been observed in
canola proteins (Tan et al., 2011).
 CYTA JOURNAL OF FOOD 5

Figure 2. Effect of pH on the protein solubility of jackfruit seed flour. Data are the mean standard deviation of three replicates. Mean values labeled with
different letters are significantly different (p < 0.05).

Figura 2. Efecto del pH en la solubilidad de protena de la harina de semilla de jaca. Los datos son el promedio desviacin estndar de tres rplicas. Los
valores promedio etiquetados con diferentes letras son significativamente distintos (p < 0,05).

Protein extraction from defatted jackfruit seed flour 606.1, protein 207.7, ash 69.1 and fat 117.1. The proximal com-
position reported for jackfruit seed flour by the author men-
Figure 2 shows the effect of the extraction pH on the protein
tioned above shows significant differences with respect to the
solubility from the defatted jackfruit seed flour. According to
results of this study; these differences were likely because the
the results, the maximal protein solubility was 80% at pH 12
seeds come from different jackfruit varieties or because the
and the minimal protein solubility was 19.4% at pH 4, which
jackfruit flour analyzed in this study was defatted. Conversely,
was considered to be the isoelectric point. The results of the
the protein composition of jackfruit seed protein isolate (JSPI)
maximal of protein extraction at pH 12 for the defatted jackfruit
and of JPIU was 844.3 and 952.1 g/kg (as dry basis), respectively,
seed flour from this study were similar to the results obtained
which indicates the beneficial effect of ultrasound treatment on
from physic nut seed cake, which had an extraction of 81.7% at
the protein concentration: an increases of 12.77%. Preece,
pH 12, whereas the lowest protein extraction was at pH 4.0
Hooshyar, Krijgsman, Fryer, and Zuidamb (2016) reported that
(Saetae, Kleekayai, Jayasena, & Suntornsuk, 2011). Therefore, a
the effect of ultrasound on separation and extraction of soy
pH of 12.0 was selected as the pH with the highest extraction
protein intensies the extraction of valuable components from
yield and was used for preparation of the protein isolates.
soybeans, leading to improved yields of protein, oil and solids of
ca. 10% after 1 min treatment. According to the microstructural
analysis undertaken in the study mentioned above, the
Proximal composition of protein isolate improved solubility was the main cause of the improved yields
upon ultrasound treatment, and not cell disruption as is fre-
Table 1 shows the proximal composition of the defatted jackfruit
quently stated in the literature. In other study, the protein yield
seed flour and the protein isolates obtained in this study.
(%) and content (%) of duck liver protein isolate from conven-
Adetolu (2008) reported the following proximal composition
tional extraction and ultrasound assisted extraction were
(g/kg as dry basis) for jackfruit seed flour: total carbohydrates
increased from 42.6 to 74.5 and from 76.5 to 80.2, respectively
(Zou et al., 2017).
The protein content of JPIU in this study was greater than
Table 1. Proximal composition (as dry basis) of jackfruit seed flour (JSF),
jackfruit seed protein isolate (JSPI) and jackfruit seed protein isolate treated the protein content of other protein isolates from fruit seed.
with ultrasound (JPIU).a Wani, Sogi, Singh, and Shivhare (2011) reported that the pro-
Tabla 1. Composicin proximal (en base seca) de la harina de semilla de jaca tein contents as dry basis were 837. and 790.5 g/kg for protein
(HSJ), aislado protenico de semilla de jaca (APSJ), y aislado protenico de isolates from watermelon seeds of the Mateera and Sugar baby
semilla de jaca tratado con ultrasonido (APJU).a varieties, respectively, whereas the protein contents of the
Component JSF JSPI JPIU protein isolates from wild apricot kernel press cake (Sharma,
Fat (g/kg) 8.1 1.9a 2.6 0.1b 0.8 0.2c Tilakratne, & Gupta, 2010) and tomato seeds (Savadkoohi &
Ash (g/kg) 38.2 0.8a 10.3 1.7b 16.1 1.9c
Protein (N 6.5) (g/kg) 140.4 2.5a 844.3 7.0b 952.1 0.1c Farahnaky, 2012) were 765.8 and 821.5 g/kg, respectively.
Total carbohydrates (g/kg) 813.3 2.6a 142.8 5.5b 31.0 6.4c
a
Each value is expressed as the mean standard deviation (n = 3). Means
with different letters within a row are significantly different (p < 0.05). Color and apparent density
a
Cada valor se expresa como promedio desviacin estndar (n = 3). Los
promedios con diferentes letras en una misma fila son significativamente The color values L*, a* and b* of JPIU are shown in Table 2.
distintos (p < 0,05). The JPIU in this study was darker in color (L* = 65.14,
6 J. A. ULLOA ET AL.

Table 2. Color and apparent density of the jackfruit seed protein isolate
treated with ultrasound (JPIU).a
Tabla 2. Color y densidad aparente del aislado protenico de semilla de jaca
tratado con ultrasonido (APJU).a
Property Value
L* (Lightness) 65.14
a* (Rednessgreenness) 5.16
b* (Yellownessblueness) 23.17
Apparent density (g/ml) 0.36
a
Each value is expressed as the mean standard deviation (n = 3).
a
Cada valor se expresa como promedio desviacin estndar (n = 3).
a* = 5.16, b* = 23.17) than the safflower protein isolate
obtained by ultrafiltration (L* = 78.12, a* = 0.63,
b* = 20.01) (Ulloa, Rosas-Ulloa, & Ulloa-Rangel, 2011) but
lighter than the physic nut seed protein isolate (L* = 36.05,
a* = 3.60, b* = 5.95) (Saetae et al., 2011). The apparent
density of JPIU was 0.46 g/ml (Table 2). The apparent density
depends on the combined effects of interrelated factors,
such as the attractive forces between particles, the particle
size and the number of contact points between the particles.
The apparent densities of the protein isolates from tomato
seeds (Liadakis, Tzia, Oreopoulou, & Thomopoulos, 1998) and
passion fruit seeds (Martnez, Medina, & Zambrano, 2011)
were 0.33 and 0.43 g/mm, respectively, which are less than
the apparent density of JPIU in this study.
Amino acid composition and protein quality
The results of the amino acid profile of JPIU are presented in
Table 3. Total essential amino acid content of JPIU is slightly
lower than the total nonessential amino acid content, which
implies that it may be considered as a moderately good
source of essential nutrients for human (Azeez, Lasekan,
Jinap, & Sulaiman, 2015). From total content of essential
amino acids of JPIU, total content of aromatic amino acids
(phenylalanine + tyrosine, 15.96 g/16 g N) was highest
followed of total content of sulfur amino acids (methio-
nine + cysteine, 7.06 g/16 g N), threonine (5.79 g/16 g N)
and lysine (5.72 g/16 g), but such values are higher than the
requirement of FAO/WHO. Food and Agriculture
Organization of the United Nations/World Health
0.38 Organization (1991) for adults. On the other hand, and con-
0.78
0.69
sidering the lower values of amino acid scores (Table 3), the
0.01 first, second and third limiting amino acids for JPIU were
valine, isoleucine and leucine, respectively, being 76.00,
80.25 and 98.43. Therefore, considering the amino acids
requirements of FAO/WHO. Food and Agriculture
Organization of the United Nations/World Health
Organization (1991) standard for adults, the proteins of
JPIU have a good balance of essential amino acids. With
respect to the predicted PER, the value obtained for the
JPIU of this study was 2.36, which is higher than the values
2.29, 2.14 and 2.04 for the protein isolates of kabuli chickpea,
desi chickpea and soy, respectively (Wang et al., 2010).
Water and oil absorption capacity and emulsifying
capacity
The factors affecting the water binding capacity of the pro-
tein include the amino acid composition, the protein con-
formation, the surface polarity and the surface
hydrophobicity. The JPIU in this study had a water absorp-
tion capacity of 6.46 ml water/g protein (Table 4), which is
greater than the values of 3.22 ml water/g protein, 3.57 ml
water/g protein and 3.13 ml water/g protein of physic nut
protein isolate (Saetae et al., 2011) and watermelon seed
protein isolates from Sugar baby and Mateera varieties,
respectively (Wani et al., 2011). This result indicates that
JPIU had good water binding capacity possibly due to the
interactions between polar amino acid residues of the pro-
tein and molecules of water. The water absorption capacity
is a critical property of proteins in viscous foods such as
soups, doughs, custards and baked products because these
foods are supposed to absorb water without protein

Table 3. Amino acid composition and nutritive quality of jackfruit seed protein isolate treated with ultrasound (JPIU).
Tabla 3. Composicin de aminocidos y calidad nutritiva del aislado protenico de semilla de jaca tratado con ultrasonido (APJU).
Jackfruit protein
Amino acid isolate (g/16 g N) Amino acid score FAO/WHO (1991) reference for adults
Essential amino acids
Lysine 5.72 0.10 104.00 4.45 5.5
Methionine +cystine 7.06 0.07 201.71 7.83 3.5
Cystine 6.48 0.05
Threonine 5.79 0.08 144.75 6.39 4.0
Isoleucine 3.21 0.07 80.25 3.85 4.0
Tryptophan Not determined Not determined 1.0
Valine 3.80 0.07 76.00 3.79 5.0
Leucine 6.89 0.05 98.43 2.79 7.0
Phenylalanine + tyrosine 15.96 0.08 266.00 7.24 6.0
Phenylalanine 7.64 0.07
Total essential amino acids 48.43 0.12
Nonessential amino acids
Arginine 12.24 0.06
Aspartic acid 7.58 0.05
Serine 9.99 0.09
Glutamic acid 8.23 0.06
Proline 2.13 0.07
Glycine 5.27 0.09
Alanine 4.06 0.05
Histidine 2.07 0.04
Total nonessential amino acids 51.57 0.14
Predicted PER 2.36 0.07

Table 4. Some functional properties of the jackfruit seed protein isolate
treated with ultrasound (JPIU).a
Tabla 4. Algunas propiedades funcionales del aislado protenico de semilla de
jaca tratado con ultrasonido (APJU).a
Property Value
Water absorption capacity (ml water/g protein) 6.46 0.65
Oil absorption capacity (ml oil/g protein) 6.07 0.36
Emulsifying capacity (ml oil/g protein) 32.26 0.70
a
Each value is expressed as the mean standard deviation (n = 3).
a
Cada valor se expresa como promedio desviacin estndar (n = 3).
dissolution, which thereby provides body, thickening and
viscosity (Seena & Sridhar, 2005).
The oil binding capacity is another important functional
property of proteins in food systems. Nonpolar amino acid
side chains of proteins can form hydrophobic interactions
with lipid hydrocarbon chains that affect the oil binding
capacity. The oil absorption capacity of JPIU was 6.07 ml
oil/g protein (Table 4), which is greater than the values of
1.86 ml oil/g protein for physic nut protein isolate (Saetae
et al., 2011), 2.37 ml oil/g protein and 2.49 ml oil/g protein
for watermelon seed protein isolates from Sugar baby and
Mateera varieties (Seena & Sridhar, 2005), 3.2 ml oil/g protein
for guava seed protein isolate (Bernardino Nicanor et al.,
2001) and 4.04 ml oil/g protein for tomato seed protein
isolate (Liadakis et al., 1998). This result indicated that JPIU
had a high content of nonpolar amino acids that can bind
with lipid hydrocarbon chains. The mechanism of fat/oil
absorption can be explained as the physical entrapment of
oil. The fat/oil absorption capacity is a critical determinant of
flavor retention. A high oil absorption capacity of protein is
required in the formulation of ground meat and of replace-
ments and extenders for use in products such as doughnuts,
baked goods, frankfurters, sausages and soups (Kaur &
Singh, 2007; Singh, Kumar, & Bawa, 2008).
JPIU had an emulsifying capacity of 32.36 ml oil/g protein
(Table 4). Previous reports have indicated that the emulsify-
ing capacity is 115 ml oil/g protein, 164169 ml oil/g protein
Figure 3. Effect of pH on the protein solubility of the jackfruit seed protein isolate. Data are the mean standard deviation of three replicates. Mean values
labeled with different letters are significantly different (p < 0.05).
Figura 3. Efecto del pH en la solubilidad del aislado protenico de semilla de jaca. Los datos son el promedio desviacin estndar de tres rplicas. Los valores
promedio etiquetados con diferentes letras son significativamente distintos (p < 0,05).
CYTA JOURNAL OF FOOD 7
and 130 ml oil/g protein for tomato seed (Liadakis et al.,
1998), lupin (El-Adawy, Rahma, El-Bedawey, & Gafar, 2001)
and sesame (Khalid, Babiker, & El Tinay, 2003) protein iso-
lates, respectively. Therefore, the JPIU exhibited a lower
emulsifying capacity than these other plant proteins.
Protein solubility of the protein isolate
Protein solubility relates to the surface hydrophobic (pro-
teinprotein) and hydrophilic (proteinsolvent) interactions
with water. It is affected by several factors, for example, the
composition of the amino acids and the non-amino acids of
the protein, the native or denatured state of the proteins
and environmental factors (Saetae et al., 2011). The pH is an
important environmental factor that has a significant effect
on the solubility of proteins. The protein solubility of JPIU as
a function of pH is shown in Figure 3. The data show two
regions of protein solubility: at acidic pH, which includes the
isoelectric point, and at alkaline pH. The minimum protein
solubility was observed at pH 4 (5.2%), which indicates the
isoelectric point of the protein; at pH 7 and 11, 44.0% and
94.4% of the protein were soluble. These results suggest that
JPIU has good solubility under basic conditions, which
agrees with the results for the protein isolate obtained
from physic nut seed cake (Saetae et al., 2011). The protein
solubility at different pH values may serve as a useful indi-
cator of the performance of protein isolates in food systems
in addition to the extent of protein denaturation as a result
of heat or chemical treatment. Most plant proteins have
isoelectric pH values between 4 and 5. At the isoelectric
point, there is no net charge on the protein; as a result,
there are no repulsive interactions or proteinprotein inter-
actions disfavoring solubility. At a low pH, large net charges
are induced and the repulsive forces increase, which results
in protein unfolding. At a pH greater than 6.5, all plant
proteins have solubilities of >70% (Bora, 2002); however, in
this study, we observed lower values.
8 J. A. ULLOA ET AL.
Least gelation concentration
The least gelation concentration indicates the gelation capa-
city; thus, a lower least gelation concentration improves the
gelling ability of proteins. The gel formation of a protein is
the result of the partial denaturation of proteins as well as
protein aggregation. Protein denaturation allows for the
exposure of reactive groups inside protein molecules, and
aggregation improves water retention into the three-dimen-
sional network structure of the proteins reactive sides
(Withana-Gamge, Wanasundara, Pietrasik, & Shand, 2010).
The least or lowest gelation concentration of proteins from
JPIU was 9% at pH 6 (Figure 4). The least gelation concen-
trations of chickpea protein, northern bean protein concen-
trate, cowpea, mung bean protein isolate, lupin seed protein
(Kaur & Singh, 2007) and safflower protein isolate (Ulloa
et al., 2011) are 1418%, 8%, 12%, 10%, 14% and 2%,
respectively.
EA and emulsion stability
Protein molecules are generally composed of nonpolar
amino acids, charged amino acids and non-charged polar
amino acids. These types of amino acid cause hydrophobic
and hydrophilic properties such that proteins can interact
with both oil and water molecules and act as emulsifiers. The
emulsifying properties of JPIU are shown in Figure 5. In our
study, the lowest values of the EA and the emulsion stability
occurred at pH 4 and 2, respectively, which can be attributed
to the low solubility of proteins at these pH values.
Conversely, the EA (127%) and emulsion stability (127%) for
JPIU were greater at pH 10 and 410, respectively, whereas
the higher EA and emulsion stability for tomato seed protein
isolate were 36.4% and 34.9%, respectively (Liadakis et al.,
1998). The emulsifying properties of JPIU exhibit a similar
pH-dependent behavior to the flaxseed protein concentrate
(Martnez et al., 2006), the safflower protein isolate (Ulloa
Figure 4. Effect of pH on the least gelation concentration of the jackfruit seed protein isolate. Data are the mean standard deviation of three replicates. Mean
values labeled with different letters are significantly different (p < 0.05).
Figura 4. Efecto del pH en la concentracin mnima de gelacin del aislado protenico de semilla de jaca. Los datos son el promedio desviacin estndar de
tres rplicas. Los valores promedio etiquetados con diferentes letras son significativamente distintos (p < 0,05).
et al., 2011) and the physic nut seed protein isolate (Saetae
et al., 2011).
Foaming capacity and FS
In food systems, foams are often very complex and include
several phases, such as a mixture of gases, subdivided solids
and liquids and multicomponent solutions of water, poly-
mers and surfactants. The foam capacity of JPIU was pH
dependent, as shown in Figure 6. The foam capacity was
found to be low in the range of pH 4.06.0 with values of
1342%, and the lowest value was at pH 4. The foam capa-
city of the protein isolate increased when subject to basic pH
conditions and reached a maximum at pH 10 (254%). Greater
values appear to be due to increasing solubility and
increased net charges of JPIU where the hydrophobic inter-
actions are weak and the flexibility of protein is increased.
This caused increasing protein diffusion to the airwater
interface for encapsulating air particles and enhancing
foam formation. The maximum foaming capacity (254%)
and FS (164%) were observed at pH 10, whereas the mini-
mum foaming capacity (13%) and FS (68%) occurred at pH 4
and 8, respectively. In contrast to the results obtained in this
study, the foaming capacity and stability of lupin protein
concentrate were greatest at acidic pH values (Sathe,
Deshpande, & Salunkhe, 1982). The maximum foaming capa-
city and FS for guava seed (Bernardino-Nicanor et al., 2001)
and tomato seed (Liadakis et al., 1998) isolates were 50%
and 40% and 64.9% and 66.3%, respectively. The major
protein molecules of jackfruit seed may be globular proteins,
which are difficult to surface denature and cause low foam
capacity (Saetae et al., 2011). The foam capacity is usually an
important factor in food products such as bread, cakes,
toppings, whipped cream, ice cream, chiffon desserts and
some confectionery products (Singh et al., 2008). Viewed as
a whole, JPIU could be considered to act as a great foaming
ingredient in different food products.
 CYTA JOURNAL OF FOOD 9

Figure 5. Effect of pH on the emulsifying activity and the emulsion stability of the jackfruit seed protein isolate. Data are the mean standard deviation of
three replicates. Mean values labeled with different letters are significantly different (p < 0.05).

Figura 5. Efecto del pH en la actividad emulsificante y estabilidad de la emulsion del aislado protenico de semilla de jaca. Los datos son el promedio
desviacin estndar de tres rplicas. Los valores promedio etiquetados con diferentes letras son significativamente distintos (p < 0,05).

Figure 6. Effect of pH on the foaming capacity and the foam stability of the jackfruit seed protein isolate. Data are the mean standard deviation of three
replicates. Mean values labeled with different letters are significantly different (p < 0.05).

Figura 6. Efecto del pH en la capacidad espumante y estabilidad de la espuma del aislado protenico de semilla de jaca. Los datos son el promedio desviacin
estndar de tres rplicas. Los valores promedio etiquetados con diferentes letras son significativamente distintos (p < 0,05).

Conclusions breads, cakes, toppings, beverages, whipped cream, ice

Jackfruit seed, a by-product of the fruit industry, is a
potential raw material for the production of a protein
isolate when subjected to ultrasound treatment. The JPIU
showed good functional properties in terms of its water
and oil binding capacity, protein solubility, gelation, emul-
sifying and foaming, in addition a good balance of essen-
tial amino acids which place it as of regular nutritive
quality. Therefore, JPIU could be a novel protein source
applied in food systems and may be suitable to add to
cream, chiffon desserts, salad dressing, sausage and meat
products.
Acknowledgments
The authors would like to acknowledge the National Council for
Science and Technology of Mexico for a scholarship for M.C.
Villalobos Barbosa. We are grateful to the Mexican Tropical Organics
S. de R.L. de C.V. for kindly providing jackfruit seeds as the working
material.
10 J. A. ULLOA ET AL.
Disclosure statement
No potential conflict of interest was reported by the authors.
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