Cloning, purification and characterization of a thermostable amylosucrase from Deinococcus geothermalis

被引：47

作者：

Emond, Stephane ^{[1
,2
,3
,4
,5
]}

Mondeil, Sophie ^{[1
,2
,3
,4
,5
]}

Jaziri, Kais ^{[1
,2
,3
,4
,5
]}

Andre, Isabelle ^{[1
,2
,3
,4
,5
]}

Monsan, Pierre ^{[1
,2
,3
,4
,5
]}

Remaud-Simeon, Magali ^{[1
,2
,3
,4
,5
]}

Potocki-Veronese, Gabrielle ^{[1
,2
,3
,4
,5
]}

机构：

[1] INSA, UPS, INP, F-31400 Toulouse, France

[2] Univ Toulouse, Toulouse, France

[3] LISBP, Toulouse, France

[4] INRA, Ingn Syst Biol & Procedes UMR792, F-31931 Toulouse, France

[5] CNRS, UMR5504, Toulouse, France

来源：

FEMS MICROBIOLOGY LETTERS | 2008年 / 285卷 / 01期

关键词：

amylosucrase; Deinococcus geothermalis; recombinant expression; amylopolysaccharide; amylose synthesis; thermostability;

D O I：

10.1111/j.1574-6968.2008.01204.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Amylosucrase is a transglucosidase that catalyses the synthesis of an amylose-type polymer from sucrose, an abundant agro-resource. Here we describe a novel thermostable amylosucrase from the moderate thermophile Deinococcus geothermalis (DGAS). The dgas gene was cloned and expressed in Escherichia coli. The encoded enzyme was purified and characterized. DGAS displays a specific activity of 44 U mg(-1), an optimal temperature of 50 degrees C and a half-life of 26 h at 50 degrees C. Moreover, it produces an alpha-glucan at 50 degrees C, with an average degree of polymerization of 45 and a polymerization yield of 76%. DGAS is thus the most active and thermostable amylosucrase known to date.

引用

页码：25 / 32

页数：8

共 23 条

[1] Molecular basis of the amylose-like polymer formation catalyzed by Neisseria polysaccharea amylosucrase [J].