Žuža, Milena

Link to this page

Authority KeyName Variants
571fc447-0c4b-453f-90d1-34a3cbfb0c10
  • Žuža, Milena (1)
Projects

Author's Bibliography

Biochemical and funcional properties of egg white hydrolysates produced by different proteases

Knežević-Jugović, Zorica; Žuža, Milena; Gluvić, Ana; Jovanović, Jelena; Stefanović, Andrea; Manojlović, Verica; Bugarski, Branko

(Belgrade : Serbian Chemical Society, 2013)

TY  - CONF
AU  - Knežević-Jugović, Zorica
AU  - Žuža, Milena
AU  - Gluvić, Ana
AU  - Jovanović, Jelena
AU  - Stefanović, Andrea
AU  - Manojlović, Verica
AU  - Bugarski, Branko
PY  - 2013
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6279
AB  - Enzymatic hydrolysis of egg white proteins (EWPs) has shown a great potential to improve their functional properties such as increased solubility, stability, and digestibility while still retaining their nutrition value. The high selectivity and mild reaction conditions associated with the enzymatic process have made this approach an attractive alternative in the production of EWPs with improved functional properties, which are often difficult to obtain by conventional chemical route. Moreover, the inherent specificity of various proteolytic enzymes should control the nature and extent of hydrolysis and thus the functional properties of the product.
The focus of this work is to find the best combination of enzymes and the mode of both substrate pretreatment and process implementation for improvement of the overall hydrolysates` quality. For this purpose EWP solution was hydrolysed with several enzymes using both, one-step and two-step hydrolysis in a stirred stirred-tank reactor employing an enzyme to protein substrate weight ratio previously selected to obtain the desired level of conversion in the first step within a time period from about 20 to about 75 minutes depending of protease used. The obtained hydrolysates were then tested on antioxidant activity, flavour, solubility, digestibility emulsifying activity, foaming capacity and stability. Selected results have been presented in Figure 1.
The application of two-step enzymatic process, based on the use of the bacterial alkaline protease in the first step, and then the introduction a more specific protease in the second step to selectively reduce the bitter peptides, seemed to be advantageous.
PB  - Belgrade : Serbian Chemical Society
C3  - Book of abstracts / 8th International Conference of the Chemical Societies of the South-East European Countries - ICOSECS
T1  - Biochemical and funcional properties of egg white hydrolysates produced by different proteases
SP  - 232
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6279
ER  - 
@conference{
author = "Knežević-Jugović, Zorica and Žuža, Milena and Gluvić, Ana and Jovanović, Jelena and Stefanović, Andrea and Manojlović, Verica and Bugarski, Branko",
year = "2013",
abstract = "Enzymatic hydrolysis of egg white proteins (EWPs) has shown a great potential to improve their functional properties such as increased solubility, stability, and digestibility while still retaining their nutrition value. The high selectivity and mild reaction conditions associated with the enzymatic process have made this approach an attractive alternative in the production of EWPs with improved functional properties, which are often difficult to obtain by conventional chemical route. Moreover, the inherent specificity of various proteolytic enzymes should control the nature and extent of hydrolysis and thus the functional properties of the product.
The focus of this work is to find the best combination of enzymes and the mode of both substrate pretreatment and process implementation for improvement of the overall hydrolysates` quality. For this purpose EWP solution was hydrolysed with several enzymes using both, one-step and two-step hydrolysis in a stirred stirred-tank reactor employing an enzyme to protein substrate weight ratio previously selected to obtain the desired level of conversion in the first step within a time period from about 20 to about 75 minutes depending of protease used. The obtained hydrolysates were then tested on antioxidant activity, flavour, solubility, digestibility emulsifying activity, foaming capacity and stability. Selected results have been presented in Figure 1.
The application of two-step enzymatic process, based on the use of the bacterial alkaline protease in the first step, and then the introduction a more specific protease in the second step to selectively reduce the bitter peptides, seemed to be advantageous.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Book of abstracts / 8th International Conference of the Chemical Societies of the South-East European Countries - ICOSECS",
title = "Biochemical and funcional properties of egg white hydrolysates produced by different proteases",
pages = "232",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6279"
}
Knežević-Jugović, Z., Žuža, M., Gluvić, A., Jovanović, J., Stefanović, A., Manojlović, V.,& Bugarski, B.. (2013). Biochemical and funcional properties of egg white hydrolysates produced by different proteases. in Book of abstracts / 8th International Conference of the Chemical Societies of the South-East European Countries - ICOSECS
Belgrade : Serbian Chemical Society., 232.
https://hdl.handle.net/21.15107/rcub_technorep_6279
Knežević-Jugović Z, Žuža M, Gluvić A, Jovanović J, Stefanović A, Manojlović V, Bugarski B. Biochemical and funcional properties of egg white hydrolysates produced by different proteases. in Book of abstracts / 8th International Conference of the Chemical Societies of the South-East European Countries - ICOSECS. 2013;:232.
https://hdl.handle.net/21.15107/rcub_technorep_6279 .
Knežević-Jugović, Zorica, Žuža, Milena, Gluvić, Ana, Jovanović, Jelena, Stefanović, Andrea, Manojlović, Verica, Bugarski, Branko, "Biochemical and funcional properties of egg white hydrolysates produced by different proteases" in Book of abstracts / 8th International Conference of the Chemical Societies of the South-East European Countries - ICOSECS (2013):232,
https://hdl.handle.net/21.15107/rcub_technorep_6279 .