Purification and characterization of two endo-beta-1,4-glucanases from Mollusca, Ampullaria crossean

	Purification and characterization of two endo-beta-1,4-glucanases from Mollusca, Ampullaria crossean
	Li, YH; Guo, R; Yin, QY; Ding, M; Zhang, SL; Xu, GJ; Zhao, FK
刊名	ACTA BIOCHIMICA ET BIOPHYSICA SINICA
	2005
卷号	37 期号:10 页码:702-708
关键词	cellulase endo-beta-1 Ampullaria crossean purification substrate specificity 4-glucanase
通讯作者	Zhao, FK (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Key Lab Proteom, Inst Biochem & Cell Biol,Grad Sch, Shanghai 200031, Peoples R China.,fkzhao@sibs.ac.cn
英文摘要	Two novel endo-beta-1,4-glucanases, EG45 and EG27, were isolated from the gastric juice of mollusca, Ampullaria crossean, by anion exchange, hydrophobic interaction, gel filtration and a second round of anion exchange chromatography. The purified proteins EG45 and EG27 appeared as a single band on sodium dodecylsulfate polyacrylamide gel electrophoresis with a molecular mass of 45 kDa and 27 kDa, respectively. The optimum pH for CMC activity was 5.5 for EG45 and 4.4-4.8 for EG27. The optimum temperature range for EG27 was broad, between 50 degrees C and 60 degrees C; for EG45 it was 50 degrees C. The analysis on the stability of these two endo-beta-1,4-glucanases showed that EG27 was acceptably stable at pH 3.0-11.0 even when the incubation time was prolonged to 24 h at 30 degrees C, whereas EG45 remained relatively stable at pH 5.0-8.0. About 85% of the activity of EG27 could be retained upon incubation at 60 degrees C for 24 h. However, less than 10% residual activity of EG45 was detected at 50 degrees C. Among different kinds of substrates, both enzymes showed a high preference for carboxymethyl cellulose. EG45, in particular, showed a carboxymethyl cellulose hydrolytic activity of 146.5 IU/mg protein. Both enzymes showed low activities to xylan (from oat spelt) and Sigmacell 101, and they were inactive to p-nitrophenyl-beta-D-cellobioside, salicin and starch.
学科主题	Biochemistry & Molecular Biology; Biophysics
类目[WOS]	Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]	NEMATODE MELOIDOGYNE-INCOGNITA ; ALKALINE CELLULASE ; ETHANOL-PRODUCTION ; MYTILUS-EDULIS ; CDNA CLONING ; BLUE MUSSEL ; ENZYMES ; GENE ; BIOTECHNOLOGY
收录类别	SCI
语种	英语
WOS记录号	WOS:000232675000008
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/1958]
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	Li, YH,Guo, R,Yin, QY,et al. Purification and characterization of two endo-beta-1,4-glucanases from Mollusca, Ampullaria crossean[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2005,37(10):702-708.
APA	Li, YH.,Guo, R.,Yin, QY.,Ding, M.,Zhang, SL.,...&Zhao, FK.(2005).Purification and characterization of two endo-beta-1,4-glucanases from Mollusca, Ampullaria crossean.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,37(10),702-708.
MLA	Li, YH,et al."Purification and characterization of two endo-beta-1,4-glucanases from Mollusca, Ampullaria crossean".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 37.10(2005):702-708.