PURIFICATION AND PROPERTIES OF A NEW RECOMBINANT CYCLODEXTRIN GLUCANOTRANSFERASE FROM E. COLI BL21 (DE3) pJCGT8-5

被引：0

作者：

Petrova, Penka ^{[1
]}

Tomova, Iva ^{[1
]}

Petrov, Kaloyan ^{[2
]}

Nikov, Iordan ^{[3
]}

Tonkova, Alexandra ^{[1
]}

机构：

[1] Bulgarian Acad Sci, Inst Microbiol, BU-1113 Sofia, Bulgaria

[2] Bulgarian Acad Sci, Inst Chem Engn, Sofia 1113, Bulgaria

[3] Univ Nord France, PolytechLille, Dep IAAL, Lab ProBioGem,UPRES EA 1026, F-59655 Villeneuve Dascq, France

来源：

COMPTES RENDUS DE L ACADEMIE BULGARE DES SCIENCES | 2013年 / 66卷 / 10期

关键词：

cyclodextrin production; E. coli BL21(DE3); enzyme purification; pJCGT8-5; recombinant cyclodextrin glucanotransferase JCGT8-5; ALKALOPHILIC BACILLUS SP; EXTRACELLULAR EXPRESSION; MOLECULAR-CLONING; ESCHERICHIA-COLI; GENE; GLYCOSYLTRANSFERASE; STRAINS; BINDING; CGTASE;

D O I：

暂无

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

A new recombinant cyclodextrin glucanotransferase JCGT8-5 (CGTase, EC 2.4.1.19) produced by E. coli BL21(DE3) cells was purified by ultrafiltraton, starch adsorption and gel filtration with a yield of 34% and displayed a specific activity 35683 U mg(-1). The purified recombinant CGTase exhibited molecular weight of 75.5 kDa estimated by SDS-PAGE. It was active at 60-65 degrees C, stable at a broad pH range (5.0-11.0) and retained more than 50% of its original activities after a heat treatment at 70 degrees C for 1 h without additives. The enzyme produced high amounts of cyclodextrins (CDs) from raw starch (12.0-12.2 mg ml(-1)) and the products formed were 22% gamma-cyclodextrin (CD), 1% alpha-CD and 77% beta-CD after 2 h incubation at 60 degrees C, without adding any selective agents.

引用

页码：1437 / 1444

页数：8

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