化学
固定化酶
壳聚糖
水解
色谱法
中性蛋白酶
酶分析
蛋白酶
酶
钠
海藻酸钙
傅里叶变换红外光谱
核化学
生物化学
有机化学
化学工程
钙
工程类
标识
DOI:10.1007/s12010-021-03773-9
摘要
Sodium alginate and chitosan were cross-linked to form composite gel spheres, which were entrapped to immobilize the free neutral protease. The matrix of the immobilized neutral protease was detected and characterized by using Fourier transform infrared spectroscopy and energy-dispersive X-ray. The optimum immobilization conditions were determined by orthogonal test, in which the concentration of sodium alginate was 3.5%, CaCl2 2.5%, chitosan 2.5%, and immobilizing time 1.5 h. Meanwhile, the activities of immobilized neutral protease and free enzyme were compared. The results showed that the pH value of immobilized enzyme was 5-8, the relative activity was above 90%, the free enzyme was above 80%, the relative activity of immobilized enzyme was above 80% in 30-80 °C, and the free enzyme was above 64% in 40-80 °C. The immobilized enzyme is better than the free enzyme in the constant of pH and temperature. The relative activity of immobilized enzyme was 50% after six hydrolysis cycles, and 80% after 11 days of storage.
科研通智能强力驱动
Strongly Powered by AbleSci AI