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
收藏
页码：1437 / 1444
页数：8
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