The acid tolerant and cold-active β-galactosidase from Lactococcus lactis strain is an attractive biocatalyst for lactose hydrolysis

被引：20

作者：

Vincent, Violette ^{[1
]}

Aghajari, Nushin ^{[1
]}

Pollet, Noemie ^{[1
]}

Boisson, Anais ^{[1
]}

Boudebbouze, Samira ^{[2
]}

Haser, Richard ^{[1
]}

Maguin, Emmanuelle ^{[2
]}

Rhimi, Moez ^{[2
]}

机构：

[1] Univ Lyon 1, Inst Biol & Chim Prot, Lab Biocrystallog & Struct Biol Therapeut Targets, Bases Mol Syst Infect UMR 5086,CNRS,FR3302, F-69367 Lyon 07, France

[2] INRA, UMR Micalis 1319, F-78350 Jouy En Josas, France

来源：

ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY | 2013年 / 103卷 / 04期

关键词：

beta-Galactosidase; Acid-tolerant; Cold-active; Immobilization; Lactose hydrolysis; POTENTIAL APPLICATION; ESCHERICHIA-COLI; GENE CLONING; PURIFICATION; BACTERIUM; IMMOBILIZATION; ALLEVIATION; EXPRESSION; RELEVANT; GLUCOSE;

D O I：

10.1007/s10482-012-9852-6

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The gene encoding the beta-galactosidase from the dairy Lactococcus lactis IL1403 strain was cloned, sequenced and overexpressed in Escherichia coli. The purified enzyme has a tetrameric arrangement composed of four identical 120 kDa subunits. Biochemical characterization showed that it is optimally active within a wide range of temperatures from 15 to 55 A degrees C and of pH from 6.0 to 7.5. For its maximal activity this enzyme requires only 0.8 mM Fe2+ and 1.6 mM Mg2+. Purified protein displayed a high catalytic efficiency of 102 s(-1) mM(-1) for lactose. The enzyme stability was increased by immobilization mainly at low pH (from 4.0 to 5.5) and high temperatures (55 and 60 A degrees C). The bioconversion of lactose using the L. lactis beta-galactosidase allows the production of lactose with a high bioconversion rate (98 %) within a wide range of pH and temperature.

引用

页码：701 / 712

页数：12

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