A novel cold-active β-D-galactosidase from the Paracoccus sp. 32d--gene cloning, purification and characterization.
Journal Title: Microbial Cell Factories - Year 2011, Vol 10, Issue
Abstract
β-D-Galactosidases (EC 3.2.1.23) catalyze the hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides. Cold-active β-D-galactosidases have recently become a focus of attention of researchers and dairy product manufactures owing to theirs ability to: (i) eliminate of lactose from refrigerated milk for people afflicted with lactose intolerance, (ii) convert lactose to glucose and galactose which increase the sweetness of milk and decreases its hydroscopicity, and (iii) eliminate lactose from dairy industry pollutants associated with environmental problems. Moreover, in contrast to commercially available mesophilic β-D-galactosidase from Kluyveromyces lactis the cold-active counterparts could make it possible both to reduce the risk of mesophiles contamination and save energy during the industrial process connected with lactose hydrolysis.
Authors and Affiliations
Anna Wierzbicka-Woś, Hubert Cieśliński, Marta Wanarska, Katarzyna Kozłowska-Tylingo, Piotr Hildebrandt, Józef Kur
Keywords
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A novel cold-active β-D-galactosidase from the Paracoccus sp. 32d--gene cloning, purification and characterization.
β-D-Galactosidases (EC 3.2.1.23) catalyze the hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides. Cold-active β-D-galactosidases have recently become a focus of attention of researchers and da...