戊二醛交联法固定扩展青霉脂肪酶的研究  

The activity of penicilium expansum lipase immobilized by cross-linking with glutaraldehyde

作　　者：王慧玲[1,2] 赵燕[1,2] 李建科[1,2] 

机构地区：[1]南昌大学生物质转化教育部工程研究中心,南昌330047 [2]南昌大学食品科学与技术国家重点实验室,南昌330047

出　　处：《食品科技》2012年第6期27-31,共5页Food Science and Technology

摘　　要：以海藻酸钠为载体,戊二醛为交联剂,采用交联吸附法固定扩展青霉脂肪酶。通过单因素试验和正交试验考察固定化主要因素对固定化酶活力的影响,优化固定化条件。结果表明,海藻酸钠浓度为3%、氯化钙为1%、戊二醛浓度为2.5%的条件下,酶浓度为0.03g/mL,pH为10.0,固定温度为40℃,固定时间为30min,该条件下固定化酶活最高为22895u/g,酶活回收率达到67.57%。在有机体系中,固定化脂肪酶的酯化能力明显高于游离态脂肪酶。在重复利用9次后,固定化脂肪酶的酶活降为初始状态的50%。In this experiment, alginate is used as carrier to immobilize penicilium expansum lipase （PEL） through crosslinking absorption method. The main elements that influence the activity of immobilized enzyme were tested to obtain optimum fixed condition through single-element experiment and orthogonal experiment. The results indicated that, with 3% alginate, 1% calcium chloride, 2.5% glutaric dialdehyde, 0.03 g/mL enzyme, 10.0 pH, 40 ℃ temperature, time 30 min, the highest activity of penicilium expansum lipase is 22895 u/g, whose reclaimed rate is 67.57%. In organic systems, the esterification ability of immobilized PEL is much stonger than that of free lipase. The activity of the immobilized lipase still kept 50% after using 9 times.

关 键 词：扩展青霉脂肪酶 固定化 海藻酸钠 回收率 

分 类 号：Q814.2[生物学—生物工程]