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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. [点击复制]
- LIN Wei-jun,ZHOU Yu-heng,JING Yan,WEI Li,QIN Xiang-xiang,ZHANG Hou-rui.Purification and Partial Properties of Laccase from Ganoderma lucidum[J].Guangxi Sciences,2009,16(1):82-86. [点击复制]
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灵芝漆酶的分离纯化及其部分酶学性质研究 |
林卫军1,2, 周玉恒1, 经艳1,2, 卫力1,2, 覃香香1, 张厚瑞1
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(1.广西植物研究所, 广西桂林 541006;2.广西师范大学生命科学学院, 广西桂林 541004) |
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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 |
DOI: |
投稿时间:2008-05-05修订日期:2008-11-17 |
基金项目:广西创新能力建设项目(No.033015-1B);广西自然科学基金项目(No.0731033)资助 |
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Purification and Partial Properties of Laccase from Ganoderma lucidum |
LIN Wei-jun1,2, ZHOU Yu-heng1, JING Yan1,2, WEI Li1,2, QIN Xiang-xiang1, ZHANG Hou-rui1
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(1.Guangxi Institute of Botany, Guilin, Guangxi, 541006, China;2.College of Life Science, Guangxi Normal University, Guilin, Guangxi, 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. |
Key words: laccase purification enzymological properties Ganoderma lucidum |