Purification of New β-Galactosidase from Enterococcus faecium MTCC 5153 with Transgalactosylation Activity.

Badarinath, V. and Prakash, M. Halami (2011) Purification of New β-Galactosidase from Enterococcus faecium MTCC 5153 with Transgalactosylation Activity. Food Biotechnology , 25. pp. 225-239.

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Abstract

A new β-galactosidase (β-gal) was purified from a lactic acid bacterial strain of Enterococcus faecium MTCC5153 by chromatographic techniques. The purified enzyme had a specific activity of 24.06 U/mg of protein with km and Vmax values of 2 mM and 18.2 mM/min/mg of protein, respectively. The yield of purified β-gal was 10.65% and estimated molecular weight found to be ∼90 kDa, consisting of two homodimeric subunits of 43kDa. The enzyme was stable in pH range of 8.0–9.0 with an optimum pH of 8 and the optimum temperature of 40◦C. The enzyme was activated in the presence of metal ions such as Mg+2, Mn+2, Ca+2, K+ and Na+ and was inhibited by Zn+2, Co+2 and Cu+2. Chemical modifiers (N-bromosuccinamide and Diethylpyro carbonate) inactivated the enzyme indicating the role of tryptophan and histidine moieties for activity. The purified β-gal was able to synthesize oligosaccharides from lactose. This study suggests that the β-gal of Enterococcus faecium MTCC5153 could be applied in dairy industry for hydrolysis of lactose and to improve its digestibility. β-gal of probiotic cultures are of particular interest due to their transgalactosylation properties.

Item Type:	Article
Uncontrolled Keywords:	E. faecium; β-galactosidase; prebiotics; transgalactosylation
Subjects:	500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
Divisions:	Food Microbiology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	05 Aug 2011 11:06
Last Modified:	23 May 2012 06:18
URI:	http://ir.cftri.res.in/id/eprint/10414

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