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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국식품영양과학회 Journal of Food Science and Nutrition Journal of Food Science and Nutrition Vol.2 No.1
- 발행연도
- 1997.3
- 수록면
- 77 - 82 (6page)
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초록· 키워드
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The comparison of soy protein coagulation by heat- and enzyme-treatment are summarized. The gelation mechanism of glycinin by heating was mainly due to dissociation and aggregation of the basic subunit of 11S globulin. In case of 75 globulin, macro-soluble aggregates may be formed by noncovalent intraction more than 30min at 80℃. Whereas, coagulum occured by the microbial enzyme was more minuter than the other Ca-, HCl-coagulum. Heat treatment attacked the basic subunit of 115 globulin and this results agreed very closely with bromelain treatment, and also it was not changed in the 75 globulin by bromelain. Microbial enzyme, however, preferred acidic subunit to basic subunit of 11s globulin and attacked the 7s globulin, that could produce coagulum products within the 4~5min at 65℃.
목차
Abstract
INTRODUCTION
SOY PROTEINS
HEAT TREATMENT
ENZYME TREATMENT
GENERAL OBSERVATION
REFERENCES
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