An alkali-stable enzyme with laccase activity from entophytic fungus and the enzymatic modification of alkali lignin

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	An alkali-stable enzyme with laccase activity from entophytic fungus and the enzymatic modification of alkali lignin
	Qiu Weihua 1,2; Chen Hongzhang 1
刊名	BIORESOURCE TECHNOLOGY
	2008-09-01
卷号	99 期号:13 页码:5480-5484
关键词	entophytic fungus alkali-stable laccase purification and characterization lignin modification
ISSN号	0960-8524
其他题名	Bioresour. Technol.
中文摘要	Mycelia Sterilia YY-5, an entophytic fungus, was isolated from Rhus chinensis Mill and its extracellular enzyme had a higher laccase activity (MS-Lac). After been purified by anion exchange and gel filtration chromatography, MS-Lac, which had a molecular mass of 45 kDa, was found to be an alkali-stable enzyme with an optimum pH of 10.0 and capable of retaining 80% activity after incubation for 72 h with syringaldazine as substrate. It was also found that syringaldazine had a higher affinity than 2,2'-azino-bis-(3-ethylbenzothiazoline)-6-sulphonate (ABTS) as substrate for MS-Lac, which was determined in sodium phosphate buffer (pH 6.0, 0.1 M) at 30 degrees C. Meanwhile, the lignin modification, catalyzed by MS-Lac, indicated that it could oxidize the phenolic hydroxyl, side chain substituent or carbonyl group of spruce alkali lignin in cetyltrimethylammonium bromide (CTAB) reversed micelles (20 mM, pH 6.0, W/O = 40) and steam-exploded wheat straw alkali lignin in NaOH solution (20 mM, pH 10.0). (C) 2007 Elsevier Ltd. All rights reserved.
英文摘要	Mycelia Sterilia YY-5, an entophytic fungus, was isolated from Rhus chinensis Mill and its extracellular enzyme had a higher laccase activity (MS-Lac). After been purified by anion exchange and gel filtration chromatography, MS-Lac, which had a molecular mass of 45 kDa, was found to be an alkali-stable enzyme with an optimum pH of 10.0 and capable of retaining 80% activity after incubation for 72 h with syringaldazine as substrate. It was also found that syringaldazine had a higher affinity than 2,2'-azino-bis-(3-ethylbenzothiazoline)-6-sulphonate (ABTS) as substrate for MS-Lac, which was determined in sodium phosphate buffer (pH 6.0, 0.1 M) at 30 degrees C. Meanwhile, the lignin modification, catalyzed by MS-Lac, indicated that it could oxidize the phenolic hydroxyl, side chain substituent or carbonyl group of spruce alkali lignin in cetyltrimethylammonium bromide (CTAB) reversed micelles (20 mM, pH 6.0, W/O = 40) and steam-exploded wheat straw alkali lignin in NaOH solution (20 mM, pH 10.0). (C) 2007 Elsevier Ltd. All rights reserved.
WOS标题词	Science & Technology ; Life Sciences & Biomedicine ; Technology
类目[WOS]	Agricultural Engineering ; Biotechnology & Applied Microbiology ; Energy & Fuels
研究领域[WOS]	Agriculture ; Biotechnology & Applied Microbiology ; Energy & Fuels
关键词[WOS]	WHITE-ROT FUNGUS ; PLEUROTUS-OSTREATUS ; MEDIATOR SYSTEMS ; WHEAT-STRAW ; OXIDATION ; PURIFICATION ; ISOENZYMES ; MN2+
收录类别	SCI
原文出处	://WOS:000256654600026
语种	英语
WOS记录号	WOS:000256654600026
公开日期	2013-10-08
内容类型	期刊论文
版本	出版稿
源URL	[http://ir.ipe.ac.cn/handle/122111/2830]
专题	过程工程研究所_研究所（批量导入）
作者单位	1.Chinese Acad Sci, State Key Lab Biochem Engn, Inst Proc Engn, Beijing 100080, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Qiu Weihua,Chen Hongzhang. An alkali-stable enzyme with laccase activity from entophytic fungus and the enzymatic modification of alkali lignin[J]. BIORESOURCE TECHNOLOGY,2008,99(13):5480-5484.
APA	Qiu Weihua,&Chen Hongzhang.(2008).An alkali-stable enzyme with laccase activity from entophytic fungus and the enzymatic modification of alkali lignin.BIORESOURCE TECHNOLOGY,99(13),5480-5484.
MLA	Qiu Weihua,et al."An alkali-stable enzyme with laccase activity from entophytic fungus and the enzymatic modification of alkali lignin".BIORESOURCE TECHNOLOGY 99.13(2008):5480-5484.