The acid tolerant and cold-active beta-galactosidase from Lactococcus lactis strain is an attractive biocatalyst for lactose hydrolysis - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Accéder directement au contenu
Article Dans Une Revue Antonie van Leeuwenhoek Année : 2013

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

Résumé

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.

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hal-01001085 , version 1 (04-06-2014)

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Violette V. Vincent, Nushin N. Aghajari, Noemie N. Pollet, Anais A. Boisson, Samira S. Boudebbouze, et al.. The acid tolerant and cold-active beta-galactosidase from Lactococcus lactis strain is an attractive biocatalyst for lactose hydrolysis. Antonie van Leeuwenhoek, 2013, 103 (4), pp.701-712. ⟨10.1007/s10482-012-9852-6⟩. ⟨hal-01001085⟩
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