Capaldo, A.Walker, M.Ford, C.Jiranek, V.2012-03-212012-03-212011Food Chemistry, 2011; 125(2):476-4820308-81461873-7072http://hdl.handle.net/2440/69986The 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.enCopyright 2010 Elsevier Ltd. All rights reserved.Phospho-b-glucosidaseOenococcus oeniPhosphoenolpyruvate-phospho transferasesystemJournal article002010167210.1016/j.foodchem.2010.09.0360002849752000272-s2.0-7804942790632846Walker, M. [0000-0002-6934-3787]Ford, C. [0000-0003-1617-2977]Jiranek, V. [0000-0002-9775-8963]