Immobilization of Lipase from Grey Mullet

被引：6

作者：

Aryee, Alberta N. A. ^{[1
]}

Simpson, Benjamin K. ^{[1
]}

机构：

[1] McGill Univ, Fac Agr & Environm Sci, Dept Food Sci & Agr Chem, Ste Anne De Bellevue, PQ H9X 3V9, Canada

来源：

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 2012年 / 168卷 / 08期

基金：

加拿大自然科学与工程研究理事会;

关键词：

Grey mullet; Delipidation; Lipase; Adsorption; Immobilization; Characterization; PURIFICATION; ENZYME; TRANSESTERIFICATION; STABILITY; VISCERA; WATER; FUEL;

D O I：

10.1007/s12010-012-9921-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Grey mullet (Mugil cephalus) lipase was isolated using para-aminobenzamidine agarose and immobilized on octyl Sepharose CL-4B (o-Sep). Immobilized grey mullet lipase (GMLi) had a 10 A degrees C higher optimum temperature compared to the free enzyme and showed remarkable thermal stability. GMLi was most active within the pH range of 8.0-9.5 with an optimum at 8.5. Immobilization also enhanced the storage stability and reusability of the enzyme with minimal changes in efficiency during repeated batches. GMLi showed variable stabilities in various organic solvents. A signal in the amide I absorption region of the FTIR spectrum of GMLi was attributed to the protein layer on o-Sep. The surface morphology of o-Sep was visualized on a Zeiss stereomicroscope as globular-shaped beads.

引用

页码：2105 / 2122

页数：18

共 37 条

[1]

Lipase fraction from the viscera of grey mullet (Mugil cephalus) -: Isolation, partial purification and some biochemical characteristics [J].