COMBINED EFFECT OF PROTEASE AND PHYTASE ON THE SOLUBILITY OF MODIFIED SOY PROTEIN

Citations

WEB OF SCIENCE

12
Citations

SCOPUS

15

초록

Soy protein isolate (SPI) was subjected to enzymatic hydrolysis with protease and phytase, and the solubilities of the modified SPIs (MSPIs) were characterized and compared with those of a commercial modified protein (SUPRO 670 IP from the Solae Company, St. Louis, MO). The solubilities of MSPIs showed a typical pH-dependent curve, shifting upward with an increase of hydrolysis time and enzyme dose. In particular, the solubility at pH 4.5 of the MSPI with degree of hydrolysis of 9.8% increased 9.7-fold more than SPI. Furthermore, the combined enzymatic treatment (protease and phytase) led to a significantly increased solubility of SPI at pH 4.5, which improved by 11.5-fold and 1.8-fold more than SPI and SUPRO 670 IP, respectively. In conclusion, the use of hydrolytic enzymes to synergistically improve solubility in the acidic range of pH may provide a positive impact on the MSPIs as a multifunctional food ingredient. Practical ApplicationsEven though soy protein isolates (SPIs) are used in food industry because of their beneficial health effects as well as specific functional properties, the applications of SPIs to processed foods under acidic conditions are very limited. In this study, SPIs were modified by each or combined enzymatic treatments and their solubilities were compared in a wide range of pH. The solubility of the modified SPI (MSPI) was significantly improved compared with the commercial product. Therefore, the MSPI with enhanced solubility at acidic pH could be used in an extended range of processed foods.

키워드

FUNCTIONAL-PROPERTIESEMULSIFYING PROPERTIESPHYTIC ACIDENZYMATIC-HYDROLYSISFOOD PROTEINSPROTEOLYSISPHOSPHORUSBITTERNESSPEPTIDESCALCIUM
제목
COMBINED EFFECT OF PROTEASE AND PHYTASE ON THE SOLUBILITY OF MODIFIED SOY PROTEIN
저자
Bae, In YoungKim, Jeong HyeongLee, Hyeon Gyu
DOI
10.1111/jfbc.12001
발행일
2013-10
유형
Article
저널명
Journal of Food Biochemistry
37
5
페이지
511 ~ 519