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Sensors 2006, 6(9), 1087-1101; doi:10.3390/s6091087
Article
Effect of Limited Hydrolysis on Traditional Soy Protein Concentrate
Institute for Food Technology, Faculty of Agriculture, University of Belgrade, Nemanjina 6, Serbia
* Author to whom correspondence should be addressed.
Received: 15 June 2006 / Accepted: 15 September 2006 / Published: 17 September 2006
Abstract: The influence of limited proteolysis of soy protein concentrate on proteinextractability, the composition of the extractable proteins, their emulsifying properties andsome nutritional properties were investigated. Traditional concentrate (alcohol leachedconcentrate) was hydrolyzed using trypsin and pepsin as hydrolytic agents. Significantdifferences in extractable protein composition between traditional concentrate and theirhydrolysates were observed by polyacrylamide gel electrophoresis (PAGE) and by SDSPAGE.All hydrolysates showed better extractability than the original protein concentrate,whereas significantly better emulsifying properties were noticed at modified concentratesobtained by trypsin induced hydrolysis. These improved properties are the result of twosimultaneous processes, dissociation and degradation of insoluble alcohol-induced proteinaggregates. Enzyme induced hydrolysis had no influence on trypsin-inibitor activity, andsignificantly reduced phytic acid content.
Keywords: limited hydrolysis; soy protein concentrate; extractability; protein composition; trypsin-inhibitor activity; phytic acid.
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MDPI and ACS Style
Barac, M.B.; Jovanovic, S.T.; Stanojevic, S.P.; Pesic, M.B. Effect of Limited Hydrolysis on Traditional Soy Protein Concentrate. Sensors 2006, 6, 1087-1101.
AMA StyleBarac MB, Jovanovic ST, Stanojevic SP, Pesic MB. Effect of Limited Hydrolysis on Traditional Soy Protein Concentrate. Sensors. 2006; 6(9):1087-1101.
Chicago/Turabian StyleBarac, Miroljub B.; Jovanovic, Snezana T.; Stanojevic, Sladjana P.; Pesic, Mirjana B. 2006. "Effect of Limited Hydrolysis on Traditional Soy Protein Concentrate." Sensors 6, no. 9: 1087-1101.
