β-Glucoside metabolism in Oenococcus oeni: Cloning and characterisation of the phospho-β-glucosidase bglD
Date
2011
Authors
Capaldo, A.
Walker, M.
Ford, C.
Jiranek, V.
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Journal article
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Food Chemistry, 2011; 125(2):476-482
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A. Capaldo, M.E. Walker, C.M. Ford and V. Jiranek
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Abstract
The structural gene for a phospho-β-glucosidase from the oenologically important lactic acid bacterium (LAB) Oenococcus oeni has been cloned and its protein product characterised. This gene is found in a putative β-glucosidase operon of 2178 base pairs encoding 4 genes designated bglA to bglD. The bglA, B and C genes were not cloned and characterised, however, are thought to be phosphoenolpyruvate dependent phospho transferase system (PEP-PTS) components IIC, IIA and IIB which regulate the uptake, phosphorylation and translocation of β-glucosides across the cytoplasmic membrane. The cloned bglD was sequenced and expressed in Escherichia coli followed by purification. The purified bglD protein has 480 residues, a molecular mass of 55.5kDa and shows high homology to known phospho-β-glucosidases. bglD exhibited high activity towards the phosphorylated β-glucoside para-nitrophenol-β-d-glucopyranoside-6-phosphate with a pH optimum of 5.5 and maintained similar levels of activity between temperatures of 4°C and 40°C. The enzyme was not active against non-phosphorylated β-glucosides.
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Copyright 2010 Elsevier Ltd. All rights reserved.