Dewei Song, Min Chen, Haiming Cheng
The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu, 610065, China.
National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, 610065, China.
Appl Biochem Biotechnol. 2016 Nov;180(5):826-840. doi: 10.1007/s12010-016-2136-2. Epub 2016 May 17.
Candida rugosa lipases were immobilized onto collagen fibers through glutaraldehyde cross-linking method. The immobilization process has been optimized. Under the optimal immobilization conditions, the activity of the collagen-immobilized lipase reached 340 U/g. The activity was recovered of 28.3 % by immobilization. The operational stability of the obtained collagen-immobilized lipase for hydrolysis of olive oil emulsion was determined. The collagen-immobilized lipase showed good tolerance to temperature and pH variations in comparison to free lipase. The collagen-immobilized lipase was also applied as biocatalyst for synthesis of butyl butyrate from butyric acid and 1-butanol in n-hexane. The conversion yield was 94 % at the optimal conditions. Of its initial activity, 64 % was retained after 5 cycles for synthesizing butyl butyrate in n-hexane.
通过戊二醛交联法将皱褶假丝酵母脂肪酶固定在胶原纤维上。对固定化过程进行了优化。在最佳固定化条件下，胶原固定化脂肪酶的活性达到340 U/g。固定化后活性回收率为28.3%。测定了所得胶原固定化脂肪酶对橄榄油乳液水解的操作稳定性。与游离脂肪酶相比，胶原固定化脂肪酶对温度和pH变化表现出良好的耐受性。胶原固定化脂肪酶还用作生物催化剂，由丁酸和正丁醇在正己烷中合成丁酸丁酯。在最佳条件下转化率为94%。在正己烷中合成丁酸丁酯5个循环后，保留了其初始活性的64%。
