The attractive recombinant phytase from Bacillus licheniformis: biochemical and molecular characterization

被引：26
作者：
Borgi, Mohamed Ali [1 ]
Boudebbouze, Samira [2 ]
Aghajari, Nushin [3 ]
Szukala, Florette [2 ]
Pons, Nicolas [2 ]
Maguin, Emmanuelle [2 ]
Rhimi, Moez [2 ]
机构：
[1] Fac Sci Gafsa, Dept Life Sci, Unit Macromol Biochem & Genet, Zarroug 2112, Gafsa, Tunisia
[2] INRA, UMR Micalis 1319, F-78350 Jouy En Josas, France
[3] Univ Lyon, CNRS, Lab Biocrystallog & Struct Biol Therapeut Targets, BMSSI Inst Biol & Chim Prot,UMR 5086,Biosci Gerla, F-69367 Lyon 07, France
来源：
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2014年 / 98卷 / 13期
关键词：
Phytase; Bacillus licheniformis ATCC 14580; Specific activity; Thermostability; Cold active enzyme; SITE-DIRECTED MUTAGENESIS; ALKALINE PHYTASE; GENE CLONING; PHYTIC ACID; EXTRACELLULAR PHYTASE; MICROBIAL PHYTASE; EXPRESSION; OVEREXPRESSION; PURIFICATION; PHOSPHORUS;
D O I：
10.1007/s00253-013-5421-9
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
The phyL gene encoding phytase from the industrial strain Bacillus licheniformis ATCC 14580 (PhyL) was cloned, sequenced, and overexpressed in Escherichia coli. Biochemical characterization demonstrated that the recombinant enzyme has an apparent molecular weight of nearly 42 kDa. Interestingly, this enzyme was optimally active at 70-75 A degrees C and pH 6.5-7.0. This enzyme is distinguishable by the fact that it preserved more than 40 % of its activity at wide range of temperatures from 4 to 85 A degrees C. This new phytase displayed also a high specific activity of 316 U/mg. For its maximal activity and thermostability, this biocatalyst required only 0.6 mM of Ca2+ ion and exhibited high catalytic efficiency of 8.3 s(-1) mu M-1 towards phytic acid.
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收藏
页码：5937 / 5947
页数：11
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