| Autor: |
Katarina G. Kanurić, Spasenija D. Milanović, Edward T. Petri, Dajana V. Hrnjez, Vladimir R. Vukić, Mirela D. Iličić |
| Jazyk: |
angličtina |
| Rok vydání: |
2015 |
| Předmět: |
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| Zdroj: |
Food Biotechnology. 29(3):248-262 |
| ISSN: |
0890-5436 |
| DOI: |
10.1080/08905436.2015.1059766 |
| Popis: |
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 fram... |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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