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灵芝漆酶的分离纯化及其部分酶学性质研究
引用本文:林卫军,周玉恒,经艳,卫力,覃香香,张厚瑞.灵芝漆酶的分离纯化及其部分酶学性质研究[J].广西科学,2009,16(1):82-86.
作者姓名:林卫军  周玉恒  经艳  卫力  覃香香  张厚瑞
作者单位:1. 广西植物研究所,广西桂林,541006;广西师范大学生命科学学院,广西桂林,541004
2. 广西植物研究所,广西桂林,541006
基金项目:广西创新能力建设项目,广西自然科学基金 
摘    要:将灵芝(Ganoderma lucidum)漆酶经过Sephadex G-75和DEAE-Sepharose Fast Flow两步纯化,获得具有3个同工酶的组分,并且纯度提高了81倍,酶活回收率高达83.9%。以ABTS为底物,漆酶最适pH值是2.2~2.6,在pH值4.6~7.8范围内稳定;最适温度45℃,在低于45℃时较稳定。大部分金属离子、酸根离子对灵芝漆酶普遍有抑制作用,除盐可以提高漆酶活力。

关 键 词:漆酶  纯化  酶学性质  灵芝
收稿时间:2008/5/5 0:00:00
修稿时间:2008/11/17 0:00:00

Purification and Partial Properties of Laccase from Ganoderma lucidum
LIN Wei-jun,ZHOU Yu-heng,JING Yan,WEI Li,QIN Xiang-xiang and ZHANG Hou-rui.Purification and Partial Properties of Laccase from Ganoderma lucidum[J].Guangxi Sciences,2009,16(1):82-86.
Authors:LIN Wei-jun  ZHOU Yu-heng  JING Yan  WEI Li  QIN Xiang-xiang and ZHANG Hou-rui
Institution:1.Guangxi Institute of Botany;Guilin;Guangxi;541006;China;2.College of Life Science;Guangxi Normal University;541004;China
Abstract:After the crude laccase from Ganoderma lucidum was purified by Sephadex G-75 gel filtration and DEAE-Sepharose Fast Flow ion exchange column chromatography, a final yield of 83.9% and a specific activity of 81-fold were achieved. The results of native polyacrylamide gel electrophoresis(PAGE) with active staining showed that there were three kinds of isoenzymes. The optimum pH value of purified laccase was between 2.2-2.6 with ABTS as substrate and the optimum temperature was 45℃. When the temperature was below 45℃ and the pH value was in the range of 4.6~ 7.8,the laccases exhibited maximal stability. Laccases from Ganoderma lucidum were universally inhibited by metal and acid ions, and desalting facilitated the activity.
Keywords:laccase  purification  enzymological properties  Ganoderma lucidum  
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