摘要
蚕丝蛋白经高压高温水脱胶后所得的丝胶溶液 ,经过纯化、浓缩以及喷雾干燥 ,制成丝胶蛋白粉末 .这种丝胶蛋白分子质量高达 2 0 0ku ,其粉末呈白色 ,平均粒度 10 μm ,为热水溶性蛋白 .以这种丝胶蛋白粉末为载体 ,用戊二醛为交联剂 ,制成固定化 L 天冬酰胺酶 .对这种固定化酶活性和动力学性质进行初步研究和分析 ,结果表明这种固定化酶性能稳定 ,对热的稳定性有所提高 ,并具有较好的操作稳定性 。
Silk sericin protein powder can be produced from the sericin solution by the processing of degumming in the high temperature and high pressure conditions, purifying, condensing and spray drying. Molecular mass of the sericin protein is high up to 200 ku. Taking on white color and about 10 μm average granularity, the powder of the protein is hot water soluble. L Asparaginase was immobilized on the natural silk sericin powder by cross linked with glutaraldehyde. The enzyme activity and dynamical properties of the immobilized L asparaginase were described. It was found that the immobilized enzyme is very stable, and the stability to heat increased in comparison with free enzyme, and this immobilized enzyme has preferable stability of operation. The resistance to trypsin hydrolysis was also improved greatly compared to that of soluble enzyme.
出处
《生物化学与生物物理进展》
SCIE
CAS
CSCD
北大核心
2002年第6期961-965,共5页
Progress In Biochemistry and Biophysics
基金
江苏省"丝绸工程"重点实验室和苏州大学"2 11"工程资助项目~~