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脂肪酶Lip2在蚕丝表面交联固定及其催化性质

邓冬梅 潘淑兰 劳振华 孙宇飞

广西科技大学学报2018,Vol.29Issue(2):84-90,7.
广西科技大学学报2018,Vol.29Issue(2):84-90,7.DOI:10.16375/j.cnki.cn45-1395/t.2018.02.13

脂肪酶Lip2在蚕丝表面交联固定及其催化性质

Cross-linking immobilization of lipase Lip2 on silk fibrin surface and its catalytic properties

邓冬梅 1潘淑兰 2劳振华 1孙宇飞2

作者信息

  • 1. 广西科技大学 生物与化学工程学院,广西 柳州545006
  • 2. 广西糖资源绿色加工重点实验室(广西科技大学),广西 柳州545006
  • 折叠

摘要

Abstract

In order to develop a low cost and high-efficiency immobilized enzyme carrier based on silk fibrin, three kinds of cross-linking agents,carbodiimide hydrochloride(EDC)N-hydroxysuccinimide(NHS)and glutar-aldehyde(GA),were used to crosslink Yarrowia lipolytica lipase Lip2 on the silk fibrin surface and the catalytic property of immobilized Lip2 was investigated. The silk fibrin carrier was activated by EDC/NHS,GA,EDC/NHS+GA respectively prior to crosslink with Lip2.The immobilization Lip2 were severally named as Lip2(EDC/NHS),Lip2(GA)and Lip2(EDC/NHS+GA).Results show that Lip2(GA)possessed the best special activity but enzyme amount it carried was poor,and conversely,Lip2(EDC/NHS+GA)carried most enzyme particle but its special activity was the lowest among them.The optimum pH value of all immobilized enzymes was 8.03,a little alkaline-shift compared with free Lip2.The optimum temperature of immobilized and free enzymes was 40℃,ex-cept Lip2(EDC/NHS)which was 50℃.The optimal K+concentration for all immobilized enzymes was 0.10 mol· L-1,less than that of Lip2(0.15 mol·L-1).The activated effect of Ca2+concentration was the same to all enzymes, no matter immobilized or free.The Cl-concentration did not affect the activity of all enzymes.The thermo stability of Lip2(GA)and the re-use property of Lip2(EDC/NHS+GA)was the best in each field.

关键词

蚕丝/固定化酶/脂肪酶/交联

Key words

silk fibrin/immobilized enzyme/lipase/cross-linking

分类

生物科学

引用本文复制引用

邓冬梅,潘淑兰,劳振华,孙宇飞..脂肪酶Lip2在蚕丝表面交联固定及其催化性质[J].广西科技大学学报,2018,29(2):84-90,7.

基金项目

广西高校糖资源加工重点实验室开放课题(2015TZYKF06) (2015TZYKF06)

广西科技大学"大学生创新创业训练计划"项目(201610594043)资助. (201610594043)

广西科技大学学报

1004-6410

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