The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates

	The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates
	Ding, M; Teng, YG; Yin, QY; Zhao, J; Zhao, FK
刊名	ACTA BIOCHIMICA ET BIOPHYSICA SINICA
	2008
卷号	40 期号:11 页码:949-954
关键词	endo-beta-1 4-glucanase endo-beta-1 4-xylanase pNPCase CMCase EGXA Ampullaria crossean cellulose-binding domain
通讯作者	Zhao, FK (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Key Lab Prote, Shanghai 20031, Peoples R China.,fkzhou@sibs.ac.cn
英文摘要	A full-length EGXA enzyme from a mollusk, Ampullaria crossean, was cloned into pFastBac vector and then heterogeneously expressed in insect Tn5 cells. Its natural N-terminal signal peptide worked well in the insect Tn5 cells. The recombinant EGXA was a 63 kDa protein and had active endo-beta-1,4-glucanase (EC 3.2.1.4) and e ndo-beta-1,4-xylanase (EC 3.2.1.8). The sp ecific activity of endo-beta-1, 4-xyla nase was higher than in the EGX, which was purified from the stomach tissues of Ampullaria crossen. The N-terminal cellulose-binding domain of EGXA made it bind to cellulose and xylan more efficiently. This cellulose-binding domain also increased the thermal stability of this recombinant enzyme and decreased the recombinant EGXA's specific activities on p-nitrophenyl-beta-D-cellobioside and sodium carboxymethyl cellulose.
学科主题	Biochemistry & Molecular Biology ; Biophysics
类目[WOS]	Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]	GENE ; MOLLUSK ; ENDO-BETA-1,4-GLUCANASES ; CELLULASES ; EXPRESSION ; CLONING ; ORIGIN
收录类别	SCI
语种	英语
WOS记录号	WOS:000261324400006
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/1451]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Ding, M,Teng, YG,Yin, QY,et al. The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2008,40(11):949-954.
APA	Ding, M,Teng, YG,Yin, QY,Zhao, J,&Zhao, FK.(2008).The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,40(11),949-954.
MLA	Ding, M,et al."The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 40.11(2008):949-954.