Purification and characterization of a recombinant β-galactosidase with transgalactosylation activity from Bifidobacterium infantis HL96

@article{Hung2002PurificationAC,
  title={Purification and characterization of a recombinant β-galactosidase with transgalactosylation activity from Bifidobacterium infantis HL96},
  author={M.-N. Hung and Bokhui Lee},
  journal={Applied Microbiology and Biotechnology},
  year={2002},
  volume={58},
  pages={439-445}
}
A β-galactosidase isoenzyme, β-GalI, from Bifidobacterium infantis HL96, was expressed in Escherichia coli and purified to homogeneity. The molecular mass of the β-GalI subunit was estimated to be 115 kDa by SDS-PAGE. The enzyme appeared to be a tetramer, with a molecular weight of about 470 kDa by native PAGE. The optimum temperature and pH for o-nitrophenyl-β-D-galactopyranoside (ONPG) and lactose were 60°C, pH 7.5, and 50°C, pH 7.5, respectively. The enzyme was stable over a pH range of 5.0… CONTINUE READING

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