Purification and Characterization of 6-Phospho-β-galactosidase fromLactobacillus gasseriJCM 1031 | Zendy

M. Suzuki | Zendy; Tadao Saito | Zendy; Takatoshi Itoh | Zendy

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Purification and Characterization of 6-Phospho-β-galactosidase fromLactobacillus gasseriJCM 1031

Author(s) -

M. Suzuki,

Tadao Saito,

Takatoshi Itoh

Publication year - 1996

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.60.139

Subject(s) - isoelectric point , lactobacillus gasseri , chemistry , enzyme , lactobacillus , molecular mass , chromatography , phosphate , pi , biochemistry , microbiology and biotechnology , biology , fermentation

6-Phospho-beta-galactosidase from Lactobacillus gasseri JCM 1031 was purified from lactobacilli to homogeneity, about 118-fold, with 0.5% recovery by several chromatographies. The molecular mass and isoelectric point of the purified enzyme were 58 kDa and pI 5.5, respectively. The Km and Vmax for o-nitrophenyl-beta-D-galactopyranoside-6-phosphate were 0.8 mM and 116.4 mumol/min/mg, respectively. Reducing agent, Fe2+ ion, and EDTA activated but PCMB, Zn2+, and Hg2+ ions strongly inhibited the enzymatic activity.

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