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Catalytic esterification performance of protease in micro-aqueous system
Biotechnology Letters ( IF 2.7 ) Pub Date : 2020-07-13 , DOI: 10.1007/s10529-020-02965-3
Junqing Qian 1 , Lihong Gou 1 , Xiaohua Zhao 1 , Changyan Zhao 1 , Hui Guo 1 , Yudong Shan 1
Affiliation  

To evaluate the catalytic esterification performance of proteases in micro-aqueous systems and to study the suitable conditions for maintaining protease activity. It was found that the protease showed better enzyme catalytic activity in the micro-aqueous phase containing 4% boric acid-borax buffer than that of the pure organic phase. The protease activity was easily activated by 0.20 M boric acid-borax buffer, and the enzyme activity was still high for a long time in alkaline environment (pH 8.40–9.60) and under the temperature of 40–55 °C. Experiments using protease and Candida lipase to synthesize sucrose-6-ethyl ester showed that protease had better esterification activity than Candida lipase in the micro-aqueous phase.

中文翻译:

蛋白酶在微水体系中的催化酯化性能

评价蛋白酶在微水体系中的催化酯化性能,研究维持蛋白酶活性的适宜条件。发现蛋白酶在含4%硼酸-硼砂缓冲液的微水相中比纯有机相表现出更好的酶催化活性。蛋白酶活性很容易被0.20 M的硼酸-硼砂缓冲液激活,在碱性环境(pH 8.40-9.60)和40-55°C的温度下,酶活性仍然很高。用蛋白酶和念珠菌脂肪酶合成蔗糖6-乙酯的实验表明,蛋白酶在微水相中比念珠菌脂肪酶具有更好的酯化活性。
更新日期:2020-07-13
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