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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국식품영양과학회 Journal of Food Science and Nutrition Journal of Food Science and Nutrition Vol.5 No.4
- 발행연도
- 2000.12
- 수록면
- 200 - 204 (5page)
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초록· 키워드
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Protein conjugation of curdlan belonging to β-1,3-glucan was carried out to improve its surface functionalities. The glucan was mixed with phosvitin, α_s-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and the resulting powder was incubated at 60℃ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. Conjugation with unfolding proteins, i.e., phosvitin and α_s-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbumin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the α_s-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and α_s-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.
목차
Abstract
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
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