Please use this identifier to cite or link to this item: https://open.uns.ac.rs/handle/123456789/31541
Title: Comparative molecular modelling and docking analysis of β-galactosidase enzymes from commercially important starter cultures used in the dairy industry
Authors: Vladimir Vukić 
Hrnjez Dajana 
Milanović Spasenija
Iličić Mirela
Kanurić Katarina
Petri Edward 
Issue Date: 2015
Journal: Food Biotechnology
Abstract: Copyright © Taylor & Francis Group, LLC. β-Galactosidases from S. thermophillus, L. acidophilus, and B. animalis lactis are essential enzymes which hydrolyze lactose during commercial yogurt and cheese production. S. thermophillus β-galactosidase is active in the human digestive tract, improving digestion in lactose-intolerant individuals. Because X-ray crystal structures have not been determined, molecular models of these β-galactosidases were created for comparative structural analysis and molecular docking against lactose. Modeling and docking results were validated using crystal structures of homologous β-galactosidase enzymes from E. coli and B. circulans. The structure of E.coli β-galactosidase in complex with lactose was used as a docking control. Structure-based sequence alignment and molecular docking identified catalytically active residues as GLU458/GLU546 in S. thermophillus, GLU148/GLU307 in L. acidophilus and GLU164/GLU324 in B. animalis ssp. lactis, and predicts residues involved in lactose recognition. These models provide a framework for future engineering of improved β-galactosidase variants with commercial applications.
URI: https://open.uns.ac.rs/handle/123456789/31541
ISSN: 0890-5436
DOI: 10.1080/08905436.2015.1059766
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