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.
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 . .
