TY  - CONF
AU  - Knežević-Jugović, Zorica
AU  - Jovanović, Jelena
AU  - Stefanović, Andrea
AU  - Grbavčić, Sanja
AU  - Šekuljica, Nataša
AU  - Elmalimadi, Mohamed B.
AU  - Bugarski, Branko
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6271
AB  - Wheat gluten is a relatively inexpensive industrial byproduct from wheat starch processing, and in
Europe also from manufacturing of bioethanol fuel. Egg producers are also faced with problems of
excess of egg white because mayonnaise industry and bakery industry use relatively high egg yolk
amounts and egg white is the remainder. Of high importance is the production of new value-added
products based on gluten and/or egg white proteins with improved properties and specialized functionality to be used in food and biobased consumer products. The objective of this research was a production of both wheat gluten and egg white protein hydrolysates with improved antioxidant properties. For this purpose, both substrates were pretreated by thermal treatment and then intensively hydrolysed with a commercial food-grade bacterial protease, Alcalase. Thus, the obtained hydrolysates were further separated by sequential ultrafiltration into four peptide fraction viz. Fraction I (> 30kDa), II (10 - 30 kDa), III (1 - 10 kDa) and IV (< 1kDa) which were investigated in terms of their antioxidant activity. The antioxidant activity of hydrolysates and peptide fractions were evaluated using 1,1-diphenyl-2-picrylhydrazyl (DPPH), 2,2′-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) radical scavenging assays and measuring ferric reducing antioxidant power assay. Scavenging of 2,2′- diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) by Fraction III, prepared with gluten protein was found to be significantly higher than other gluten or egg white fractions. The results show that the fractionated hydrolysates were superior to the original hydrolysate in the antioxidative activity tested in all cases and can be concluded that by combining thermal pretreatment and controlled enzymatic hydrolysis, the hydrolysates with improved antioxidant properties can be produced enhancing utilization of egg white and gluten in food products.
PB  - Bratislava, SK : Slovak Society of Chemical Engineering
C3  - Proceedings / 42nd International Conference of SSCHE Tatranské Matliare
T1  - Hydrolysis of egg white and wheat proteins with protease from bacillus licheniformis: fractionation and identification of bioactive peptides
SP  - 753
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6271
ER  - 

@conference{
author = "Knežević-Jugović, Zorica and Jovanović, Jelena and Stefanović, Andrea and Grbavčić, Sanja and Šekuljica, Nataša and Elmalimadi, Mohamed B. and Bugarski, Branko",
year = "2015",
abstract = "Wheat gluten is a relatively inexpensive industrial byproduct from wheat starch processing, and in
Europe also from manufacturing of bioethanol fuel. Egg producers are also faced with problems of
excess of egg white because mayonnaise industry and bakery industry use relatively high egg yolk
amounts and egg white is the remainder. Of high importance is the production of new value-added
products based on gluten and/or egg white proteins with improved properties and specialized functionality to be used in food and biobased consumer products. The objective of this research was a production of both wheat gluten and egg white protein hydrolysates with improved antioxidant properties. For this purpose, both substrates were pretreated by thermal treatment and then intensively hydrolysed with a commercial food-grade bacterial protease, Alcalase. Thus, the obtained hydrolysates were further separated by sequential ultrafiltration into four peptide fraction viz. Fraction I (> 30kDa), II (10 - 30 kDa), III (1 - 10 kDa) and IV (< 1kDa) which were investigated in terms of their antioxidant activity. The antioxidant activity of hydrolysates and peptide fractions were evaluated using 1,1-diphenyl-2-picrylhydrazyl (DPPH), 2,2′-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) radical scavenging assays and measuring ferric reducing antioxidant power assay. Scavenging of 2,2′- diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azinobis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) by Fraction III, prepared with gluten protein was found to be significantly higher than other gluten or egg white fractions. The results show that the fractionated hydrolysates were superior to the original hydrolysate in the antioxidative activity tested in all cases and can be concluded that by combining thermal pretreatment and controlled enzymatic hydrolysis, the hydrolysates with improved antioxidant properties can be produced enhancing utilization of egg white and gluten in food products.",
publisher = "Bratislava, SK : Slovak Society of Chemical Engineering",
journal = "Proceedings / 42nd International Conference of SSCHE Tatranské Matliare",
title = "Hydrolysis of egg white and wheat proteins with protease from bacillus licheniformis: fractionation and identification of bioactive peptides",
pages = "753",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6271"
}

Knežević-Jugović, Z., Jovanović, J., Stefanović, A., Grbavčić, S., Šekuljica, N., Elmalimadi, M. B.,& Bugarski, B.. (2015). Hydrolysis of egg white and wheat proteins with protease from bacillus licheniformis: fractionation and identification of bioactive peptides. in Proceedings / 42nd International Conference of SSCHE Tatranské Matliare
Bratislava, SK : Slovak Society of Chemical Engineering., 753.
https://hdl.handle.net/21.15107/rcub_technorep_6271

Knežević-Jugović Z, Jovanović J, Stefanović A, Grbavčić S, Šekuljica N, Elmalimadi MB, Bugarski B. Hydrolysis of egg white and wheat proteins with protease from bacillus licheniformis: fractionation and identification of bioactive peptides. in Proceedings / 42nd International Conference of SSCHE Tatranské Matliare. 2015;:753.
https://hdl.handle.net/21.15107/rcub_technorep_6271 .

Knežević-Jugović, Zorica, Jovanović, Jelena, Stefanović, Andrea, Grbavčić, Sanja, Šekuljica, Nataša, Elmalimadi, Mohamed B., Bugarski, Branko, "Hydrolysis of egg white and wheat proteins with protease from bacillus licheniformis: fractionation and identification of bioactive peptides" in Proceedings / 42nd International Conference of SSCHE Tatranské Matliare (2015):753,
https://hdl.handle.net/21.15107/rcub_technorep_6271 .

TY  - CONF
AU  - Jovanović, Jelena
AU  - Stefanović, Andrea
AU  - Grbavčić, Sanja
AU  - Šekuljica, Nataša
AU  - Elmalimadi, Mohamed B.
AU  - Bugarski, Branko
AU  - Knežević-Jugović, Zorica
PY  - 2015
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6275
AB  - This contribution was aimed at the fractionation and identification of peptides with improved
antimicrobial activity from egg white protein hydrolysates, obtained by membrane ultrafiltration. For
this purpose, the thermal treated egg white proteins were intensively hydrolysed with a commercial
food-grade bacterial endopeptidase from Bacillus licheniformis, namely Alcalase. Thus, obtained
hydrolysates were further separated by sequential ultrafiltration into four peptide fractions viz. fraction I (> 30kDa), II (10 - 30 kDa), III (1 - 10 kDa) and IV (< 1kDa) which were investigated in terms of their antimicrobial activity. The antimicrobial activity was tested against Gram-positive bacteria (Staphylococcus aureus ATCC 25923), Gram-negative bacteria (Escherichia coli ATCC 25922) and against yeast Candida albicans (ATCC 24433) by fractions' susceptibility of agar diffusion. Our results showed that these peptide fractions have an intense inhibitory activity on Gram-positive bacteria, poor on Gram-negative bacteria and none inhibitory activity on growth of C. albicans. The results showed interesting antimicrobial potentials versus the tested microorganisms, especially fractions with peptides molecular weight of 10-30 kDa and 1-10 kDa. It can be concluded, that the controlled enzymatic hydrolysis of egg white proteins and their subsequent membrane ultrafiltration is considered to be a suitable way for production of biocative peptides with exhibit antimicrobial efficiency.
PB  - Bratislava, SK : Slovak Society of Chemical Engineering
C3  - Proceedings / 42nd International Conference of Slovak Society of Chemical Engineering
T1  - Peptides with improved antimicrobial activity screened by membrane ultrafiltration from egg white protein hydrolysates
EP  - 739
SP  - 732
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6275
ER  - 

@conference{
author = "Jovanović, Jelena and Stefanović, Andrea and Grbavčić, Sanja and Šekuljica, Nataša and Elmalimadi, Mohamed B. and Bugarski, Branko and Knežević-Jugović, Zorica",
year = "2015",
abstract = "This contribution was aimed at the fractionation and identification of peptides with improved
antimicrobial activity from egg white protein hydrolysates, obtained by membrane ultrafiltration. For
this purpose, the thermal treated egg white proteins were intensively hydrolysed with a commercial
food-grade bacterial endopeptidase from Bacillus licheniformis, namely Alcalase. Thus, obtained
hydrolysates were further separated by sequential ultrafiltration into four peptide fractions viz. fraction I (> 30kDa), II (10 - 30 kDa), III (1 - 10 kDa) and IV (< 1kDa) which were investigated in terms of their antimicrobial activity. The antimicrobial activity was tested against Gram-positive bacteria (Staphylococcus aureus ATCC 25923), Gram-negative bacteria (Escherichia coli ATCC 25922) and against yeast Candida albicans (ATCC 24433) by fractions' susceptibility of agar diffusion. Our results showed that these peptide fractions have an intense inhibitory activity on Gram-positive bacteria, poor on Gram-negative bacteria and none inhibitory activity on growth of C. albicans. The results showed interesting antimicrobial potentials versus the tested microorganisms, especially fractions with peptides molecular weight of 10-30 kDa and 1-10 kDa. It can be concluded, that the controlled enzymatic hydrolysis of egg white proteins and their subsequent membrane ultrafiltration is considered to be a suitable way for production of biocative peptides with exhibit antimicrobial efficiency.",
publisher = "Bratislava, SK : Slovak Society of Chemical Engineering",
journal = "Proceedings / 42nd International Conference of Slovak Society of Chemical Engineering",
title = "Peptides with improved antimicrobial activity screened by membrane ultrafiltration from egg white protein hydrolysates",
pages = "739-732",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6275"
}

Jovanović, J., Stefanović, A., Grbavčić, S., Šekuljica, N., Elmalimadi, M. B., Bugarski, B.,& Knežević-Jugović, Z.. (2015). Peptides with improved antimicrobial activity screened by membrane ultrafiltration from egg white protein hydrolysates. in Proceedings / 42nd International Conference of Slovak Society of Chemical Engineering
Bratislava, SK : Slovak Society of Chemical Engineering., 732-739.
https://hdl.handle.net/21.15107/rcub_technorep_6275

Jovanović J, Stefanović A, Grbavčić S, Šekuljica N, Elmalimadi MB, Bugarski B, Knežević-Jugović Z. Peptides with improved antimicrobial activity screened by membrane ultrafiltration from egg white protein hydrolysates. in Proceedings / 42nd International Conference of Slovak Society of Chemical Engineering. 2015;:732-739.
https://hdl.handle.net/21.15107/rcub_technorep_6275 .

Jovanović, Jelena, Stefanović, Andrea, Grbavčić, Sanja, Šekuljica, Nataša, Elmalimadi, Mohamed B., Bugarski, Branko, Knežević-Jugović, Zorica, "Peptides with improved antimicrobial activity screened by membrane ultrafiltration from egg white protein hydrolysates" in Proceedings / 42nd International Conference of Slovak Society of Chemical Engineering (2015):732-739,
https://hdl.handle.net/21.15107/rcub_technorep_6275 .

TY  - CONF
AU  - Jovanović, Jelena
AU  - Stefanović, Andrea
AU  - Jakovetić Tanasković, Sonja
AU  - Luković, Nevena
AU  - Šekuljica, Nataša
AU  - Žuža Praštalo, Milena
AU  - Knežević-Jugović, Zorica
PY  - 2014
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6277
AB  - The objective of this study was to investigate the effect of ultrasound pretreatment on two-step enzymatic hydrolysis of egg white proteins (EWPs) using commercial food-grade proteases as well as evaluating some functional properties of obtained hydrolysates. 
Three commercially available proteases used in this work were: alcalase from Bacillus licheniformis, neutrase from Bacillus amyloliquefaciens and flavourzyme from Aspergillus oryzae. Thus obtained hydrolysates were further separated by sequential ultrafiltration into three peptide fraction viz. Fraction I (< 1kDa), II (1 - 10 kDa), III (10 - 30 kDa) which were investigated in terms of their antioxidant activity. The antioxidant activity of hydrolysates and peptide fractions were evaluated using 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging assay. 
Comparing the hydrolytic curves of two-step enzymatic process, the highest equilibrium degree of hydrolysis (DH) was achieved by a combination of alcalase and neutrase. The order of addition of these two proteolytic enzymes didn't lead to significant differences in the initial rate of reaction, but significantly affected the equilibrium DH (32.25 ± 2.08%). The two-step hydrolysis, in which flavourzyme is followed by alcalase, seemed to perform with the same initial rate, but DH was considerably lower (28.23 ± 0.91%). Two-step enzymatic hydrolysis appeared to increase solubility and substantially improved the foam stability while the foam capacity didn't change significantly vs. control. The high yield of peptides soluble at pH 6 and pH 8 were obtained by combination of alcalase and flavourzyme while more voluminous foams were obtained with alcalase and neutrase. The most abundant fraction in terms of antioxidant activity was the Fraction II, which indicates that the combination of alcalase and flavourzyme was efficient at reducing the pretreated into low molecular weight peptides. 
This study showed that by combining ultrasound pretreatment under controlled conditions with careful proteases selection, hydrolysates with improved functional and antioxidant properties can be produced enhancing utilization of egg white in food products.
PB  - Skopje, Macedonia : Consulting and training center - KEY
C3  - Book of Abstracts / 1st Conference on Food Quality and Safety, Health and Nutrition - NUTRICON 2014
T1  - Antioxidant activity and functional properties of peptides derived from egg white proteins by two-step enzymatic hydrolysis
EP  - 77
SP  - 76
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6277
ER  - 

@conference{
author = "Jovanović, Jelena and Stefanović, Andrea and Jakovetić Tanasković, Sonja and Luković, Nevena and Šekuljica, Nataša and Žuža Praštalo, Milena and Knežević-Jugović, Zorica",
year = "2014",
abstract = "The objective of this study was to investigate the effect of ultrasound pretreatment on two-step enzymatic hydrolysis of egg white proteins (EWPs) using commercial food-grade proteases as well as evaluating some functional properties of obtained hydrolysates. 
Three commercially available proteases used in this work were: alcalase from Bacillus licheniformis, neutrase from Bacillus amyloliquefaciens and flavourzyme from Aspergillus oryzae. Thus obtained hydrolysates were further separated by sequential ultrafiltration into three peptide fraction viz. Fraction I (< 1kDa), II (1 - 10 kDa), III (10 - 30 kDa) which were investigated in terms of their antioxidant activity. The antioxidant activity of hydrolysates and peptide fractions were evaluated using 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging assay. 
Comparing the hydrolytic curves of two-step enzymatic process, the highest equilibrium degree of hydrolysis (DH) was achieved by a combination of alcalase and neutrase. The order of addition of these two proteolytic enzymes didn't lead to significant differences in the initial rate of reaction, but significantly affected the equilibrium DH (32.25 ± 2.08%). The two-step hydrolysis, in which flavourzyme is followed by alcalase, seemed to perform with the same initial rate, but DH was considerably lower (28.23 ± 0.91%). Two-step enzymatic hydrolysis appeared to increase solubility and substantially improved the foam stability while the foam capacity didn't change significantly vs. control. The high yield of peptides soluble at pH 6 and pH 8 were obtained by combination of alcalase and flavourzyme while more voluminous foams were obtained with alcalase and neutrase. The most abundant fraction in terms of antioxidant activity was the Fraction II, which indicates that the combination of alcalase and flavourzyme was efficient at reducing the pretreated into low molecular weight peptides. 
This study showed that by combining ultrasound pretreatment under controlled conditions with careful proteases selection, hydrolysates with improved functional and antioxidant properties can be produced enhancing utilization of egg white in food products.",
publisher = "Skopje, Macedonia : Consulting and training center - KEY",
journal = "Book of Abstracts / 1st Conference on Food Quality and Safety, Health and Nutrition - NUTRICON 2014",
title = "Antioxidant activity and functional properties of peptides derived from egg white proteins by two-step enzymatic hydrolysis",
pages = "77-76",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6277"
}

Jovanović, J., Stefanović, A., Jakovetić Tanasković, S., Luković, N., Šekuljica, N., Žuža Praštalo, M.,& Knežević-Jugović, Z.. (2014). Antioxidant activity and functional properties of peptides derived from egg white proteins by two-step enzymatic hydrolysis. in Book of Abstracts / 1st Conference on Food Quality and Safety, Health and Nutrition - NUTRICON 2014
Skopje, Macedonia : Consulting and training center - KEY., 76-77.
https://hdl.handle.net/21.15107/rcub_technorep_6277

Jovanović J, Stefanović A, Jakovetić Tanasković S, Luković N, Šekuljica N, Žuža Praštalo M, Knežević-Jugović Z. Antioxidant activity and functional properties of peptides derived from egg white proteins by two-step enzymatic hydrolysis. in Book of Abstracts / 1st Conference on Food Quality and Safety, Health and Nutrition - NUTRICON 2014. 2014;:76-77.
https://hdl.handle.net/21.15107/rcub_technorep_6277 .

Jovanović, Jelena, Stefanović, Andrea, Jakovetić Tanasković, Sonja, Luković, Nevena, Šekuljica, Nataša, Žuža Praštalo, Milena, Knežević-Jugović, Zorica, "Antioxidant activity and functional properties of peptides derived from egg white proteins by two-step enzymatic hydrolysis" in Book of Abstracts / 1st Conference on Food Quality and Safety, Health and Nutrition - NUTRICON 2014 (2014):76-77,
https://hdl.handle.net/21.15107/rcub_technorep_6277 .