THERMOSTABLE BETA-GLYCOSIDASE FROM SULFOLOBUS-SOLFATARICUS

被引:27
作者
MORACCI, M
CIARAMELLA, M
NUCCI, R
PEARL, LH
SANDERSON, I
TRINCONE, A
ROSSI, M
机构
[1] INST PROT BIOCHEM & ENZYMOL,I-80125 NAPLES,ITALY
[2] IST CHIM MOLEC INTERESSE BIOL,I-80072 NAPLES,ITALY
[3] UNIV LONDON UNIV COLL,DEPT BIOCHEM & MOLEC BIOL,LONDON WC1E 6BT,ENGLAND
来源
BIOCATALYSIS | 1994年 / 11卷 / 02期
关键词
ARCHAEA; THERMOSTABLE ENZYMES; BETA-GLUCOSIDASE; EXPRESSION IN MESOPHILIC HOSTS; SEQUENCE HOMOLOGY; CRYSTAL STRUCTURE; GLYCOSIDES; ENZYMATIC SYNTHESIS;
D O I
10.3109/10242429409034380
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Sulfolobus solfataricus beta-glycosidase (S beta gly) is a thermostable and thermophilic glycosyl-hydrolase with broad substrate specificity. The enzyme hydrolizes beta-D-gluco-, fuco-, and galactosides, and a large number of beta-linked glycoside dimers and oligomers, linked beta 1-3, beta 1-4, and beta 1-6, It is able to hydrolize oligosaccharides with up to 5 glucose residues. Furthermore, it is also able to promote transglycosylation reactions. The corresponding gene has been cloned and overexpressed both in yeast and Escherichia coli. Based on sequence acid functional data, the S beta gly has been assigned to the so-called EGA family of glycosyl-hydrolases, including beta-glycosidases, beta-galactosidases and phosho-beta-galactosidases from mesophilic and thermophilic organisms of the three domains. The S beta gly has been crystallized and the resolution of its structure is in progress. Because of its special properties, the enzymes has considerable biotechnological potential.
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页码:89 / 103
页数:15
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