Properties and potential advantages of β-galactosidase from Bacteroides polypragmatus

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DOIResolve DOI: http://doi.org/10.1007/BF00250030
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TypeArticle
Journal titleApplied Microbiology and Biotechnology
Volume22
Issue2
Pages114120; # of pages: 7
AbstractA β-galactosidase (EC 3.2.1.23) from the mesophilic obligate anaerobe, Bacteroides polypragmatus, was purified 172 fold by p-aminophenyl-β-D-thiogalactopyranoside agarose affinity chromatography followed by Bio-Gel P300 chromatography. The presence of Mg2+ and a reducing agent such as dithiothreitol (DTT) or mercaptoethanol was required for enzyme activity. The optimum pH and temperature, as determined from hydrolysis of the substrate analogue o-nitrophenyl-β-D-galactopyranoside (ONPG), for enzyme activity were 6.8 and 45°C, respectively. There was negligible activity loss during incubation at 35°C for up to 13 h. The Km values obtained with ONPG and lactose as substrates were 0.43 mM and 9.09 mM respectively. The enzyme obtained by affinity chromatography was shown to hydrolyze the lactose component of cheese whey; the amount of lactose hydrolyzed was 32% of that expected with pure lactose as the substrate in buffer containing Mg2+ and DTT.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedNo
NRC numberPATEL1985
24295
NPARC number9370494
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Record identifier6a05ec37-f7b5-49cd-ac35-5579aae202e4
Record created2009-07-10
Record modified2016-05-09
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