|本期目录/Table of Contents|

[1]韩君莉,郭丽琼,郑晓冰,等.灵芝TR6号漆酶的分离纯化及性质研究[J].应用与环境生物学报,2008,14(01):99-103.
 HAN Junli,et al..Purification and Characterization of Fungal Laccase from Ganoderma lucidum Strain TR6[J].Chinese Journal of Applied & Environmental Biology,2008,14(01):99-103.
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灵芝TR6号漆酶的分离纯化及性质研究()
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《应用与环境生物学报》[ISSN:1006-687X/CN:51-1482/Q]

卷:
14卷
期数:
2008年01期
页码:
99-103
栏目:
综述
出版日期:
2008-01-15

文章信息/Info

Title:
Purification and Characterization of Fungal Laccase from Ganoderma lucidum Strain TR6
作者:
韩君莉郭丽琼郑晓冰周伟坚林俊芳
(华南农业大学 1生物质能研究所, 2食品学院广州510642)
Author(s):
HAN Junli et al.
(1Institute of Biomass Energy, 2College of Food Science, South China Agricultural University, Guangzhou 510642, China)
关键词:
关键词灵芝漆酶纯化酶活
Keywords:
Keywords Ganoderma lucidum laccase purification enzyme activity
摘要:
摘要 采用硫酸铵盐析、 DEAE Sepharose Fast Flow 柱层析和Sephadex G100凝胶柱层析对灵芝TR6号漆酶发酵液进行分离纯化,得到电泳纯漆酶. SDS-PAGE电泳结果显示,该漆酶表观分子量为62×103. Native-PAGE鉴定该漆酶由一种同工酶组成,为单体酶.试验结果表明,该漆酶的最适反应温度为60 ℃,与ABTS的最适反应pH为45, Km为0188 mmol/L, 在pH 60~80之间较稳定. Fe2+、 SDS和Tris对该漆酶活性具有抑制作用, EDTA和Tween80则对该漆酶活性具有促进作用. 图8 表2 参10
Abstract:
Abstract The laccase from Ganoderma lucidum strain TR6 was purified by ammonium sulfate salting out, DEAE Sepharose Fast Flow column chromatography and Sephadex G100 gel column chromatography, and the electrophoretic pure laccase was obtained. The result of SDS-PAGE showed that the apparent molecular weight of the laccase was 62×103. The result of native-PAGE indicated that the laccase was a monomeric protein with only one isoenzyme. Experimental results revealed that the optimum temperature and pH of the laccase reacted with ABTS were 60 ℃ and 45, respectively, and its Km value was 0188 mmol/L. The laccase was stable at pH ranging from 6.0 to 80. The laccase activity was strongly inhibited by Fe2+, SDS and Tris, while enhanced by EDTA and Tween 80. Fig 8, Tab 2, Ref 10

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更新日期/Last Update: 2008-03-05