Pavlićević, Milica Ž.

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orcid::0000-0001-9609-1944
  • Pavlićević, Milica Ž. (5)
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Author's Bibliography

The extraction of antioxidative compounds from rusks enriched with millet flour (Panicum miliaceum L.)

Poleksić, Dajana T.; Pavlićević, Milica Ž.; Raković-Simić, Jelena M.; Rac, Vladislav; Vučelić-Radović, Biljana; Rakić, Vesna

(Srpsko hemijsko društvo, Beograd, 2018)

TY  - JOUR
AU  - Poleksić, Dajana T.
AU  - Pavlićević, Milica Ž.
AU  - Raković-Simić, Jelena M.
AU  - Rac, Vladislav
AU  - Vučelić-Radović, Biljana
AU  - Rakić, Vesna
PY  - 2018
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/4777
AB  - Two different ways of extracting antioxidative compounds (including soluble polyphenols) from rusks made from wheat flour with added millet (Panicum miliaceum L.) were compared, i.e., solvent extraction and in vitro digestion. Wheat flour was replaced by millet flour in amounts of 10, 20 or 30 wt. % (per dry mass). Solvent extraction was realized using a mixture of ethanol and water in different percentages, with or without the addition of formic acid. The total content of phenolic compounds (TPC) was determined using Folin-Ciocalteu reagent, while the antioxidative capacity was measured by the DPPH (2,2-diphenyl-1-picrylhydrazyl) assay. The efficiency of solvent extraction was enhanced by the addition of formic acid. The addition of millet flour in amounts up to 20 % enhanced the antioxidative properties. It was shown that in vitro digestion was more efficient in the extraction of antioxidative compounds, in comparison with solvent extraction.
PB  - Srpsko hemijsko društvo, Beograd
T2  - JOURNAL OF THE SERBIAN CHEMICAL SOCIETY
T1  - The extraction of antioxidative compounds from rusks enriched with millet flour (Panicum miliaceum L.)
EP  - 732
IS  - 6
SP  - 723
VL  - 83
DO  - 10.2298/JSC171229028P
ER  - 
@article{
author = "Poleksić, Dajana T. and Pavlićević, Milica Ž. and Raković-Simić, Jelena M. and Rac, Vladislav and Vučelić-Radović, Biljana and Rakić, Vesna",
year = "2018",
abstract = "Two different ways of extracting antioxidative compounds (including soluble polyphenols) from rusks made from wheat flour with added millet (Panicum miliaceum L.) were compared, i.e., solvent extraction and in vitro digestion. Wheat flour was replaced by millet flour in amounts of 10, 20 or 30 wt. % (per dry mass). Solvent extraction was realized using a mixture of ethanol and water in different percentages, with or without the addition of formic acid. The total content of phenolic compounds (TPC) was determined using Folin-Ciocalteu reagent, while the antioxidative capacity was measured by the DPPH (2,2-diphenyl-1-picrylhydrazyl) assay. The efficiency of solvent extraction was enhanced by the addition of formic acid. The addition of millet flour in amounts up to 20 % enhanced the antioxidative properties. It was shown that in vitro digestion was more efficient in the extraction of antioxidative compounds, in comparison with solvent extraction.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "JOURNAL OF THE SERBIAN CHEMICAL SOCIETY",
title = "The extraction of antioxidative compounds from rusks enriched with millet flour (Panicum miliaceum L.)",
pages = "732-723",
number = "6",
volume = "83",
doi = "10.2298/JSC171229028P"
}
Poleksić, D. T., Pavlićević, M. Ž., Raković-Simić, J. M., Rac, V., Vučelić-Radović, B.,& Rakić, V.. (2018). The extraction of antioxidative compounds from rusks enriched with millet flour (Panicum miliaceum L.). in JOURNAL OF THE SERBIAN CHEMICAL SOCIETY
Srpsko hemijsko društvo, Beograd., 83(6), 723-732.
https://doi.org/10.2298/JSC171229028P
Poleksić DT, Pavlićević MŽ, Raković-Simić JM, Rac V, Vučelić-Radović B, Rakić V. The extraction of antioxidative compounds from rusks enriched with millet flour (Panicum miliaceum L.). in JOURNAL OF THE SERBIAN CHEMICAL SOCIETY. 2018;83(6):723-732.
doi:10.2298/JSC171229028P .
Poleksić, Dajana T., Pavlićević, Milica Ž., Raković-Simić, Jelena M., Rac, Vladislav, Vučelić-Radović, Biljana, Rakić, Vesna, "The extraction of antioxidative compounds from rusks enriched with millet flour (Panicum miliaceum L.)" in JOURNAL OF THE SERBIAN CHEMICAL SOCIETY, 83, no. 6 (2018):723-732,
https://doi.org/10.2298/JSC171229028P . .
2
1
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Evaluation of Variation in Protein Composition on Solubility, Emulsifying and Gelling Properties of Soybean Genotypes Synthesizing ' Subunit

Pavlićević, Milica Ž.; Tomić, Milos D.; Djonlagić, Jasna; Stanojević, Sladjana; Vučelić-Radović, Biljana

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Pavlićević, Milica Ž.
AU  - Tomić, Milos D.
AU  - Djonlagić, Jasna
AU  - Stanojević, Sladjana
AU  - Vučelić-Radović, Biljana
PY  - 2018
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/4747
AB  - The effects of subunit composition of two major proteins of soybean: glycinin (11S) and -conglycinin (7S) in nine different genotypes, on solubility and emulsifying and gelling properties at different pH (3, 5, 6, and 8) were examined. High-protein genotypes (more than 40%) contained low amounts of the subunit. The main factors influencing solubility at pH 6 were the content of , (r = 0.89 and r = 0.91 at P  lt  0.05, respectively) and subunit contents (r = -0.71 at P  lt  0.05) of -conglycinin, while at pH 3 acidic subunits in glycinin had a positive correlation with solubility (r = 0.69 at P  lt  0.05). Emulsion activity at pH 6 was higher for genotypes synthesizing subunit (r = 0.57 at P  lt  0.05). Genotypes synthesizing higher amounts of and subunit had higher emulsion stability at pH 6 (r = 0.85 and r = 0.92 at P  lt  0.05, respectively) and pH 8 (r = 0.91 and r = 0.97 at P  lt  0.05, respectively). The rheological measurements showed that genotypes with 11S/7S ratio higher than 2.2 formed gels with enhanced storage moduli. This influence was largely due to the high content of SH groups in glycinin acidic polypeptides resulting in stabilization of gels via disulfide bonding. Gels prepared from genotypes containing higher amounts of subunit of -conglycinin exhibited reduced elastic properties. Genotypes showing better solubility also had higher emulsion stability, but formed weaker gels and had lower emulsion activity near neutral pH.
PB  - Wiley, Hoboken
T2  - Journal of the American Oil Chemists Society
T1  - Evaluation of Variation in Protein Composition on Solubility, Emulsifying and Gelling Properties of Soybean Genotypes Synthesizing ' Subunit
EP  - 134
IS  - 2
SP  - 123
VL  - 95
DO  - 10.1002/aocs.12002
ER  - 
@article{
author = "Pavlićević, Milica Ž. and Tomić, Milos D. and Djonlagić, Jasna and Stanojević, Sladjana and Vučelić-Radović, Biljana",
year = "2018",
abstract = "The effects of subunit composition of two major proteins of soybean: glycinin (11S) and -conglycinin (7S) in nine different genotypes, on solubility and emulsifying and gelling properties at different pH (3, 5, 6, and 8) were examined. High-protein genotypes (more than 40%) contained low amounts of the subunit. The main factors influencing solubility at pH 6 were the content of , (r = 0.89 and r = 0.91 at P  lt  0.05, respectively) and subunit contents (r = -0.71 at P  lt  0.05) of -conglycinin, while at pH 3 acidic subunits in glycinin had a positive correlation with solubility (r = 0.69 at P  lt  0.05). Emulsion activity at pH 6 was higher for genotypes synthesizing subunit (r = 0.57 at P  lt  0.05). Genotypes synthesizing higher amounts of and subunit had higher emulsion stability at pH 6 (r = 0.85 and r = 0.92 at P  lt  0.05, respectively) and pH 8 (r = 0.91 and r = 0.97 at P  lt  0.05, respectively). The rheological measurements showed that genotypes with 11S/7S ratio higher than 2.2 formed gels with enhanced storage moduli. This influence was largely due to the high content of SH groups in glycinin acidic polypeptides resulting in stabilization of gels via disulfide bonding. Gels prepared from genotypes containing higher amounts of subunit of -conglycinin exhibited reduced elastic properties. Genotypes showing better solubility also had higher emulsion stability, but formed weaker gels and had lower emulsion activity near neutral pH.",
publisher = "Wiley, Hoboken",
journal = "Journal of the American Oil Chemists Society",
title = "Evaluation of Variation in Protein Composition on Solubility, Emulsifying and Gelling Properties of Soybean Genotypes Synthesizing ' Subunit",
pages = "134-123",
number = "2",
volume = "95",
doi = "10.1002/aocs.12002"
}
Pavlićević, M. Ž., Tomić, M. D., Djonlagić, J., Stanojević, S.,& Vučelić-Radović, B.. (2018). Evaluation of Variation in Protein Composition on Solubility, Emulsifying and Gelling Properties of Soybean Genotypes Synthesizing ' Subunit. in Journal of the American Oil Chemists Society
Wiley, Hoboken., 95(2), 123-134.
https://doi.org/10.1002/aocs.12002
Pavlićević MŽ, Tomić MD, Djonlagić J, Stanojević S, Vučelić-Radović B. Evaluation of Variation in Protein Composition on Solubility, Emulsifying and Gelling Properties of Soybean Genotypes Synthesizing ' Subunit. in Journal of the American Oil Chemists Society. 2018;95(2):123-134.
doi:10.1002/aocs.12002 .
Pavlićević, Milica Ž., Tomić, Milos D., Djonlagić, Jasna, Stanojević, Sladjana, Vučelić-Radović, Biljana, "Evaluation of Variation in Protein Composition on Solubility, Emulsifying and Gelling Properties of Soybean Genotypes Synthesizing ' Subunit" in Journal of the American Oil Chemists Society, 95, no. 2 (2018):123-134,
https://doi.org/10.1002/aocs.12002 . .
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2
9

Influence of extraction method on protein profile of soybeans

Pavlićević, Milica Ž.; Stanojević, Sladjana; Vučelić-Radović, Biljana

(Savez hemijskih inženjera, Beograd, 2013)

TY  - JOUR
AU  - Pavlićević, Milica Ž.
AU  - Stanojević, Sladjana
AU  - Vučelić-Radović, Biljana
PY  - 2013
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3232
AB  - Comparison between protein profiles of soybean obtained by commonly used methods of extraction (Tris buffer and Tris-urea buffer) with methods used for extraction of plant proteins for 2D PAGE analysis (direct solubilization in IEF buffer, acetone extraction, phenol extraction, extraction with urea solubilization buffer and thiourea-urea extraction) was investigated. 2D profiles of samples extracted directly in IEF buffer, in urea solubilization buffer and in acetone were characterized with low number of spots. Analysis of 2D PAGE profiles of Tris buffer and Tris-urea buffer extracts showed high degree of horizontal and vertical streaking. Thiourea-urea extraction gave a higher number of less intense protein spots than phenol extraction. The method of choice, due to a large number of intense spots, would be phenol extraction.
AB  - Upoređeni su profili proteina semena soje dobijeni tradicionalnim metodama ekstrakcije (Tris-HCl puffer i Tris-urea pufer) sa profilima proteina soje ekstrahovanim metodama koje se obično koriste za ekstrakciju biljnih proteina za 2D PAGE analizu (direktno rastvaranje u IEF puferu, acetonska ekstrakcija, fenolna ekstrakcija, ekstrakcija puferom sa ureom i tiourea/urea ekstrakcija). Cilj rada je bio utvrditi primenljivost ekstrakcije Tris-HCl i Tris-urea puferom u 2D PAGE analizi. Raširena primena ove dve metode ekstrakcije zasnovana je na dobijanju visoke koncentracije proteina koji se karakterišu dobrom rastvorljivošću, kao i na već dobro poznatim Rf vrednostima pojedinih proteinskih podjedinica na SDS PAGE elektroforegramima visoke rezolucije. Tako bi njihova eventualna primena u proteomiks analizama, omogućila kako brzu analizu uzoraka, tako i prikupljanje većeg broja podataka, jer bi se izbegla potreba za resolubilizacijom i gubitak proteina. Poređenje ekstrakcionih metoda vršeno je na osnovu broja rastvornih proteina u ekstraktu, kao i denzitometrijskih merenja broja, intenziteta i oštrine tačaka na 2D profilima u okviru dva različita pH opsega. Premda ekstrakcije sa Tris-HCl i Tris-urea puferom daju najveću koncentraciju proteina u ekstraktu, ove metode daju manji broj tačaka u poredjenju sa ostalim ispitivanim metodama. Takođe, izraženo vertikalno i horizontalno 'razvlačenje' onemogućavaju preciznu denzitometrijsku analizu. Dodatni nedostatak ovih metoda (pogotovu ekstrakcije sa Tris-HCl puferom) jeste produženo vreme potrebno za korak izoelektričnog fokusiranja u poredjenju sa ostalim metodama. Direktna ekstrakcija u IEF puferu i ekstrakcija puferom sa ureom daju slične rezultate i karakterišu se malim brojem difuznih tačaka. Acetonskom ekstrakcijom dobija se mala koncentracija rastvorljivih proteina, a na 2D PAGE profilima uočava se visok stepen horizontalnog razvlačenja. Tiourea- urea ekstrakcija daje veći broj manje intenzivnih tačaka u poređenju sa fenolnom ekstrakcijom. Manji intenzitet tačaka može značiti gubitak manje zastupljenih proteina. U slučaju fenolne ekstrakcije, veliki broj koraka tokom pripreme uzorka produžava vreme analize, ali su tačke najintenziivnije. Na osnovu dobijenih rezultata, zaključeno je da je fenolna ekstrakcija metoda izbora za ekstrakciju proteina iz semena soje za analizu 2D PAGE metodom.
PB  - Savez hemijskih inženjera, Beograd
T2  - Hemijska industrija
T1  - Influence of extraction method on protein profile of soybeans
T1  - Uticaj metode ekstrakcije na proteinske profile proteina soje
EP  - 694
IS  - 4
SP  - 687
VL  - 67
DO  - 10.2298/HEMIND120919115P
ER  - 
@article{
author = "Pavlićević, Milica Ž. and Stanojević, Sladjana and Vučelić-Radović, Biljana",
year = "2013",
abstract = "Comparison between protein profiles of soybean obtained by commonly used methods of extraction (Tris buffer and Tris-urea buffer) with methods used for extraction of plant proteins for 2D PAGE analysis (direct solubilization in IEF buffer, acetone extraction, phenol extraction, extraction with urea solubilization buffer and thiourea-urea extraction) was investigated. 2D profiles of samples extracted directly in IEF buffer, in urea solubilization buffer and in acetone were characterized with low number of spots. Analysis of 2D PAGE profiles of Tris buffer and Tris-urea buffer extracts showed high degree of horizontal and vertical streaking. Thiourea-urea extraction gave a higher number of less intense protein spots than phenol extraction. The method of choice, due to a large number of intense spots, would be phenol extraction., Upoređeni su profili proteina semena soje dobijeni tradicionalnim metodama ekstrakcije (Tris-HCl puffer i Tris-urea pufer) sa profilima proteina soje ekstrahovanim metodama koje se obično koriste za ekstrakciju biljnih proteina za 2D PAGE analizu (direktno rastvaranje u IEF puferu, acetonska ekstrakcija, fenolna ekstrakcija, ekstrakcija puferom sa ureom i tiourea/urea ekstrakcija). Cilj rada je bio utvrditi primenljivost ekstrakcije Tris-HCl i Tris-urea puferom u 2D PAGE analizi. Raširena primena ove dve metode ekstrakcije zasnovana je na dobijanju visoke koncentracije proteina koji se karakterišu dobrom rastvorljivošću, kao i na već dobro poznatim Rf vrednostima pojedinih proteinskih podjedinica na SDS PAGE elektroforegramima visoke rezolucije. Tako bi njihova eventualna primena u proteomiks analizama, omogućila kako brzu analizu uzoraka, tako i prikupljanje većeg broja podataka, jer bi se izbegla potreba za resolubilizacijom i gubitak proteina. Poređenje ekstrakcionih metoda vršeno je na osnovu broja rastvornih proteina u ekstraktu, kao i denzitometrijskih merenja broja, intenziteta i oštrine tačaka na 2D profilima u okviru dva različita pH opsega. Premda ekstrakcije sa Tris-HCl i Tris-urea puferom daju najveću koncentraciju proteina u ekstraktu, ove metode daju manji broj tačaka u poredjenju sa ostalim ispitivanim metodama. Takođe, izraženo vertikalno i horizontalno 'razvlačenje' onemogućavaju preciznu denzitometrijsku analizu. Dodatni nedostatak ovih metoda (pogotovu ekstrakcije sa Tris-HCl puferom) jeste produženo vreme potrebno za korak izoelektričnog fokusiranja u poredjenju sa ostalim metodama. Direktna ekstrakcija u IEF puferu i ekstrakcija puferom sa ureom daju slične rezultate i karakterišu se malim brojem difuznih tačaka. Acetonskom ekstrakcijom dobija se mala koncentracija rastvorljivih proteina, a na 2D PAGE profilima uočava se visok stepen horizontalnog razvlačenja. Tiourea- urea ekstrakcija daje veći broj manje intenzivnih tačaka u poređenju sa fenolnom ekstrakcijom. Manji intenzitet tačaka može značiti gubitak manje zastupljenih proteina. U slučaju fenolne ekstrakcije, veliki broj koraka tokom pripreme uzorka produžava vreme analize, ali su tačke najintenziivnije. Na osnovu dobijenih rezultata, zaključeno je da je fenolna ekstrakcija metoda izbora za ekstrakciju proteina iz semena soje za analizu 2D PAGE metodom.",
publisher = "Savez hemijskih inženjera, Beograd",
journal = "Hemijska industrija",
title = "Influence of extraction method on protein profile of soybeans, Uticaj metode ekstrakcije na proteinske profile proteina soje",
pages = "694-687",
number = "4",
volume = "67",
doi = "10.2298/HEMIND120919115P"
}
Pavlićević, M. Ž., Stanojević, S.,& Vučelić-Radović, B.. (2013). Influence of extraction method on protein profile of soybeans. in Hemijska industrija
Savez hemijskih inženjera, Beograd., 67(4), 687-694.
https://doi.org/10.2298/HEMIND120919115P
Pavlićević MŽ, Stanojević S, Vučelić-Radović B. Influence of extraction method on protein profile of soybeans. in Hemijska industrija. 2013;67(4):687-694.
doi:10.2298/HEMIND120919115P .
Pavlićević, Milica Ž., Stanojević, Sladjana, Vučelić-Radović, Biljana, "Influence of extraction method on protein profile of soybeans" in Hemijska industrija, 67, no. 4 (2013):687-694,
https://doi.org/10.2298/HEMIND120919115P . .
4
4
4

Functional properties of protein hydrolysates from pea (Pisum sativum, L) seeds

Barać, Miroljub; Čabrilo, Slavica B.; Stanojević, Sladjana; Pešić, Mirjana; Pavlićević, Milica Ž.; Zlatković, Branislav; Janković, Miodrag

(Wiley, Hoboken, 2012)

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 . .
56
34
56

Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin

Barać, Miroljub; Čabrilo, Slavica B.; Pešić, Mirjana; Stanojević, Sladjana; Pavlićević, Milica Ž.; Maćej, Ognjen; Ristić, Nikola

(MDPI, BASEL, 2011)

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 . .
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