TY  - JOUR
AU  - Barać, Miroljub
AU  - Pešić, Mirjana
AU  - Stanojević, Sladjana
AU  - Kostić, Aleksandar
AU  - Čabrilo, Slavica B.
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3859
AB  - Due to high nutritive quality, good techno-functional properties and low cost, legume protein products are becoming the most appropriate alternative to protein products of animal origin. In food industries, these products are usually used as techno-functional additives which provide specific characteristics of final food products. Legume proteins are commonly used as flour, concentrates, and isolates. The greatest application on industrial scale has soy proteins, and to a lesser extent, in the past 20 years, pea protein isolates. The modest use of pea protein is partly a result of insufficient information relating to their techno-functional properties. This paper is an overview of techno-functional properties of pea proteins and their isolates. Also, the paper deals with the possible use of limited enzymatic hydrolysis as a method for the improvement of their techno-functional properties.
AB  - Zahvaljujući visokoj nutritivnoj vrednosti, dobrim tehno-funkcionalnim karakteristikama i niskoj ceni, proteini leguminoza postaju najprihvatljivija alternativa za proteinske proizvode animalnog porekla. U industriji hrane ovi proizvodi najčešće se koriste kao tehno-funkcionalni aditivi kojima se obezbeđuje neka od karakteristika finalnog proizvoda. Proteini leguminoza najčešće se koriste kao proteinska brašna, koncentrati i izolati. U industrijskim razmerama najveću primenu imaju proteini soje i u znatno manjoj meri, u poslednjih 20 godina, proteinski izolati graška. Ređa upotreba proteina graška delom je posledica još uvek nedovoljno informacija o njihovim tehno-funkcionalnim karakteristikama. Ovaj rad predstavlja pregled tehno-funkcionalnih karakteristika proteina graška i njegovih izolata. Takođe, u ovom radu razmatra se i delimična proteoliza kao metod za poboljšanje tehno-funkcionalnih karakteristika proteina graška.
PB  - Univerzitet u Novom Sadu - Tehnološki fakultet, Novi Sad
T2  - Acta periodica technologica
T1  - Techno-functional properties of pea (Pisum Sativum) protein isolates: A review
T1  - Tehno-funkcionalne osobine izolata proteina graška
EP  - 18
IS  - 46
SP  - 1
DO  - 10.2298/APT1546001B
ER  - 

@article{
author = "Barać, Miroljub and Pešić, Mirjana and Stanojević, Sladjana and Kostić, Aleksandar and Čabrilo, Slavica B.",
year = "2015",
abstract = "Due to high nutritive quality, good techno-functional properties and low cost, legume protein products are becoming the most appropriate alternative to protein products of animal origin. In food industries, these products are usually used as techno-functional additives which provide specific characteristics of final food products. Legume proteins are commonly used as flour, concentrates, and isolates. The greatest application on industrial scale has soy proteins, and to a lesser extent, in the past 20 years, pea protein isolates. The modest use of pea protein is partly a result of insufficient information relating to their techno-functional properties. This paper is an overview of techno-functional properties of pea proteins and their isolates. Also, the paper deals with the possible use of limited enzymatic hydrolysis as a method for the improvement of their techno-functional properties., Zahvaljujući visokoj nutritivnoj vrednosti, dobrim tehno-funkcionalnim karakteristikama i niskoj ceni, proteini leguminoza postaju najprihvatljivija alternativa za proteinske proizvode animalnog porekla. U industriji hrane ovi proizvodi najčešće se koriste kao tehno-funkcionalni aditivi kojima se obezbeđuje neka od karakteristika finalnog proizvoda. Proteini leguminoza najčešće se koriste kao proteinska brašna, koncentrati i izolati. U industrijskim razmerama najveću primenu imaju proteini soje i u znatno manjoj meri, u poslednjih 20 godina, proteinski izolati graška. Ređa upotreba proteina graška delom je posledica još uvek nedovoljno informacija o njihovim tehno-funkcionalnim karakteristikama. Ovaj rad predstavlja pregled tehno-funkcionalnih karakteristika proteina graška i njegovih izolata. Takođe, u ovom radu razmatra se i delimična proteoliza kao metod za poboljšanje tehno-funkcionalnih karakteristika proteina graška.",
publisher = "Univerzitet u Novom Sadu - Tehnološki fakultet, Novi Sad",
journal = "Acta periodica technologica",
title = "Techno-functional properties of pea (Pisum Sativum) protein isolates: A review, Tehno-funkcionalne osobine izolata proteina graška",
pages = "18-1",
number = "46",
doi = "10.2298/APT1546001B"
}

Barać, M., Pešić, M., Stanojević, S., Kostić, A.,& Čabrilo, S. B.. (2015). Techno-functional properties of pea (Pisum Sativum) protein isolates: A review. in Acta periodica technologica
Univerzitet u Novom Sadu - Tehnološki fakultet, Novi Sad.(46), 1-18.
https://doi.org/10.2298/APT1546001B

Barać M, Pešić M, Stanojević S, Kostić A, Čabrilo SB. Techno-functional properties of pea (Pisum Sativum) protein isolates: A review. in Acta periodica technologica. 2015;(46):1-18.
doi:10.2298/APT1546001B .

Barać, Miroljub, Pešić, Mirjana, Stanojević, Sladjana, Kostić, Aleksandar, Čabrilo, Slavica B., "Techno-functional properties of pea (Pisum Sativum) protein isolates: A review" in Acta periodica technologica, no. 46 (2015):1-18,
https://doi.org/10.2298/APT1546001B . .

TY  - JOUR
AU  - Barać, Miroljub
AU  - Čabrilo, Slavica B.
AU  - Stanojević, Sladjana
AU  - Pešić, Mirjana
AU  - Pavlićević, Milica Ž.
AU  - Zlatković, Branislav
AU  - Janković, Miodrag
PY  - 2012
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/2962
AB  - The aim of this study was to investigate the effects of partial enzymatic hydrolysis on functional properties of two different pea protein isolates obtained from two pea genotypes, Maja and L1. Papain and commercial protease (Streptomyces griseus protease) were used for protein modification. Solubility, emulsifying and foaming properties were estimated at four different pH values (3.0, 5.0, 7.0 and 8.0). Papain increased solubility of L1 pea protein isolate at pH 3.0, 5.0 and 8.0, emulsifying properties and foaming capacity at all pH values. Otherwise, papain increased solubility of Maja pea protein isolate only at pH 8.0. This pea protein isolate modified with both enzymes formed emulsions with improved stability at lower pH (3.0, 5.0). The commercial protease-prepared pea protein isolates showed generally low solubility and different emulsifying and foaming properties. Proper selection of enzyme, conditions of hydrolysis and genotypes could result in production of pea protein isolates with desirable functional properties.
PB  - Wiley, Hoboken
T2  - International Journal of Food Science and Technology
T1  - Functional properties of protein hydrolysates from pea (Pisum sativum, L) seeds
EP  - 1467
IS  - 7
SP  - 1457
VL  - 47
DO  - 10.1111/j.1365-2621.2012.02993.x
ER  - 

@article{
author = "Barać, Miroljub and Čabrilo, Slavica B. and Stanojević, Sladjana and Pešić, Mirjana and Pavlićević, Milica Ž. and Zlatković, Branislav and Janković, Miodrag",
year = "2012",
abstract = "The aim of this study was to investigate the effects of partial enzymatic hydrolysis on functional properties of two different pea protein isolates obtained from two pea genotypes, Maja and L1. Papain and commercial protease (Streptomyces griseus protease) were used for protein modification. Solubility, emulsifying and foaming properties were estimated at four different pH values (3.0, 5.0, 7.0 and 8.0). Papain increased solubility of L1 pea protein isolate at pH 3.0, 5.0 and 8.0, emulsifying properties and foaming capacity at all pH values. Otherwise, papain increased solubility of Maja pea protein isolate only at pH 8.0. This pea protein isolate modified with both enzymes formed emulsions with improved stability at lower pH (3.0, 5.0). The commercial protease-prepared pea protein isolates showed generally low solubility and different emulsifying and foaming properties. Proper selection of enzyme, conditions of hydrolysis and genotypes could result in production of pea protein isolates with desirable functional properties.",
publisher = "Wiley, Hoboken",
journal = "International Journal of Food Science and Technology",
title = "Functional properties of protein hydrolysates from pea (Pisum sativum, L) seeds",
pages = "1467-1457",
number = "7",
volume = "47",
doi = "10.1111/j.1365-2621.2012.02993.x"
}

Barać, M., Čabrilo, S. B., Stanojević, S., Pešić, M., Pavlićević, M. Ž., Zlatković, B.,& Janković, M.. (2012). Functional properties of protein hydrolysates from pea (Pisum sativum, L) seeds. in International Journal of Food Science and Technology
Wiley, Hoboken., 47(7), 1457-1467.
https://doi.org/10.1111/j.1365-2621.2012.02993.x

Barać M, Čabrilo SB, Stanojević S, Pešić M, Pavlićević MŽ, Zlatković B, Janković M. Functional properties of protein hydrolysates from pea (Pisum sativum, L) seeds. in International Journal of Food Science and Technology. 2012;47(7):1457-1467.
doi:10.1111/j.1365-2621.2012.02993.x .

Barać, Miroljub, Čabrilo, Slavica B., Stanojević, Sladjana, Pešić, Mirjana, Pavlićević, Milica Ž., Zlatković, Branislav, Janković, Miodrag, "Functional properties of protein hydrolysates from pea (Pisum sativum, L) seeds" in International Journal of Food Science and Technology, 47, no. 7 (2012):1457-1467,
https://doi.org/10.1111/j.1365-2621.2012.02993.x . .

TY  - JOUR
AU  - Barać, Miroljub
AU  - Čabrilo, Slavica B.
AU  - Pešić, Mirjana
AU  - Stanojević, Sladjana
AU  - Pavlićević, Milica Ž.
AU  - Maćej, Ognjen
AU  - Ristić, Nikola
PY  - 2011
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/2678
AB  - In this paper, the effects of limited hydrolysis on functional properties, as well as on protein composition of laboratory-prepared pea protein isolates, were investigated. Pea protein isolates were hydrolyzed for either 15, 30 and 60 min with recombined chymosin (Maxiren). The effect of enzymatic action on solubility, emulsifying and foaming properties at different pH values (3.0; 5.0; 7.0 and 8.0) was monitored. Chymosin can be a very useful agent for improvement of functional properties of isolates. Action of this enzyme caused a low degree of hydrolysis (3.9-4.7%), but improved significantly functional properties of pea protein isolates (PPI), especially at lower pH values (3.0-5.0). At these pH values all hydrolysates had better solubility, emulsifying activity and foaming stability, while longer-treated samples (60 min) formed more stable emulsions at higher pH values (7.0, 8.0) than initial isolates. Also, regardless of pH value, all hydrolysates showed improved foaming ability. A moderate positive correlation between solubility and emulsifying activity index (EAI) (0.74) and negative correlation between solubility and foam stability (-0.60) as well as between foam stability (FS) and EAI (-0.77) were observed. Detected enhancement in functional properties was a result of partial hydrolysis of insoluble protein complexes.
PB  - MDPI, BASEL
T2  - International Journal of Molecular Sciences
T1  - Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin
EP  - 8387
IS  - 12
SP  - 8372
VL  - 12
DO  - 10.3390/ijms12128372
ER  - 

@article{
author = "Barać, Miroljub and Čabrilo, Slavica B. and Pešić, Mirjana and Stanojević, Sladjana and Pavlićević, Milica Ž. and Maćej, Ognjen and Ristić, Nikola",
year = "2011",
abstract = "In this paper, the effects of limited hydrolysis on functional properties, as well as on protein composition of laboratory-prepared pea protein isolates, were investigated. Pea protein isolates were hydrolyzed for either 15, 30 and 60 min with recombined chymosin (Maxiren). The effect of enzymatic action on solubility, emulsifying and foaming properties at different pH values (3.0; 5.0; 7.0 and 8.0) was monitored. Chymosin can be a very useful agent for improvement of functional properties of isolates. Action of this enzyme caused a low degree of hydrolysis (3.9-4.7%), but improved significantly functional properties of pea protein isolates (PPI), especially at lower pH values (3.0-5.0). At these pH values all hydrolysates had better solubility, emulsifying activity and foaming stability, while longer-treated samples (60 min) formed more stable emulsions at higher pH values (7.0, 8.0) than initial isolates. Also, regardless of pH value, all hydrolysates showed improved foaming ability. A moderate positive correlation between solubility and emulsifying activity index (EAI) (0.74) and negative correlation between solubility and foam stability (-0.60) as well as between foam stability (FS) and EAI (-0.77) were observed. Detected enhancement in functional properties was a result of partial hydrolysis of insoluble protein complexes.",
publisher = "MDPI, BASEL",
journal = "International Journal of Molecular Sciences",
title = "Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin",
pages = "8387-8372",
number = "12",
volume = "12",
doi = "10.3390/ijms12128372"
}

Barać, M., Čabrilo, S. B., Pešić, M., Stanojević, S., Pavlićević, M. Ž., Maćej, O.,& Ristić, N.. (2011). Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin. in International Journal of Molecular Sciences
MDPI, BASEL., 12(12), 8372-8387.
https://doi.org/10.3390/ijms12128372

Barać M, Čabrilo SB, Pešić M, Stanojević S, Pavlićević MŽ, Maćej O, Ristić N. Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin. in International Journal of Molecular Sciences. 2011;12(12):8372-8387.
doi:10.3390/ijms12128372 .

Barać, Miroljub, Čabrilo, Slavica B., Pešić, Mirjana, Stanojević, Sladjana, Pavlićević, Milica Ž., Maćej, Ognjen, Ristić, Nikola, "Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin" in International Journal of Molecular Sciences, 12, no. 12 (2011):8372-8387,
https://doi.org/10.3390/ijms12128372 . .

TY  - JOUR
AU  - Barać, Miroljub
AU  - Čabrilo, Slavica B.
AU  - Pešić, Mirjana
AU  - Stanojević, Sladjana
AU  - Žilić, Sladjana
AU  - Maćej, Ognjen
AU  - Ristić, Nikola
PY  - 2010
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/2354
AB  - Extractability, extractable protein compositions, technological-functional properties of pea (Pisum sativum) proteins from six genotypes grown in Serbia were investigated. Also, the relationship between these characteristics was presented. Investigated genotypes showed significant differences in storage protein content, composition and extractability. The ratio of vicilin: legumin concentrations, as well as the ratio of vicilin + convicilin: Legumin concentrations were positively correlated with extractability. Our data suggest that the higher level of vicilin and/or a lower level of legumin have a positive influence on protein extractability. The emulsion activity index (EAI) was strongly and positively correlated with the solubility, while no significant correlation was found between emulsion stability (ESI) and solubility, nor between foaming properties and solubility. No association was evident between ESI and EAI. A moderate positive correlation between emulsion stability and foam capacity was observed. Proteins from the investigated genotypes expressed significantly different emulsifying properties and foam capacity at different pH values, whereas low foam stability was detected. It appears that genotype has considerable influence on content, composition and technological-functional properties of pea bean proteins. This fact can be very useful for food scientists in efforts to improve the quality of peas and pea protein products.
PB  - MDPI, BASEL
T2  - International Journal of Molecular Sciences
T1  - Profile and Functional Properties of Seed Proteins from Six Pea (Pisum sativum) Genotypes
EP  - 4991
IS  - 12
SP  - 4974
VL  - 11
DO  - 10.3390/ijms11124973
ER  - 

@article{
author = "Barać, Miroljub and Čabrilo, Slavica B. and Pešić, Mirjana and Stanojević, Sladjana and Žilić, Sladjana and Maćej, Ognjen and Ristić, Nikola",
year = "2010",
abstract = "Extractability, extractable protein compositions, technological-functional properties of pea (Pisum sativum) proteins from six genotypes grown in Serbia were investigated. Also, the relationship between these characteristics was presented. Investigated genotypes showed significant differences in storage protein content, composition and extractability. The ratio of vicilin: legumin concentrations, as well as the ratio of vicilin + convicilin: Legumin concentrations were positively correlated with extractability. Our data suggest that the higher level of vicilin and/or a lower level of legumin have a positive influence on protein extractability. The emulsion activity index (EAI) was strongly and positively correlated with the solubility, while no significant correlation was found between emulsion stability (ESI) and solubility, nor between foaming properties and solubility. No association was evident between ESI and EAI. A moderate positive correlation between emulsion stability and foam capacity was observed. Proteins from the investigated genotypes expressed significantly different emulsifying properties and foam capacity at different pH values, whereas low foam stability was detected. It appears that genotype has considerable influence on content, composition and technological-functional properties of pea bean proteins. This fact can be very useful for food scientists in efforts to improve the quality of peas and pea protein products.",
publisher = "MDPI, BASEL",
journal = "International Journal of Molecular Sciences",
title = "Profile and Functional Properties of Seed Proteins from Six Pea (Pisum sativum) Genotypes",
pages = "4991-4974",
number = "12",
volume = "11",
doi = "10.3390/ijms11124973"
}

Barać, M., Čabrilo, S. B., Pešić, M., Stanojević, S., Žilić, S., Maćej, O.,& Ristić, N.. (2010). Profile and Functional Properties of Seed Proteins from Six Pea (Pisum sativum) Genotypes. in International Journal of Molecular Sciences
MDPI, BASEL., 11(12), 4974-4991.
https://doi.org/10.3390/ijms11124973

Barać M, Čabrilo SB, Pešić M, Stanojević S, Žilić S, Maćej O, Ristić N. Profile and Functional Properties of Seed Proteins from Six Pea (Pisum sativum) Genotypes. in International Journal of Molecular Sciences. 2010;11(12):4974-4991.
doi:10.3390/ijms11124973 .

Barać, Miroljub, Čabrilo, Slavica B., Pešić, Mirjana, Stanojević, Sladjana, Žilić, Sladjana, Maćej, Ognjen, Ristić, Nikola, "Profile and Functional Properties of Seed Proteins from Six Pea (Pisum sativum) Genotypes" in International Journal of Molecular Sciences, 11, no. 12 (2010):4974-4991,
https://doi.org/10.3390/ijms11124973 . .