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Properties of β-Galactosidase from Lactobacillus salivarius subsp. salivarius Nam27
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 Title & Authors
Properties of β-Galactosidase from Lactobacillus salivarius subsp. salivarius Nam27
Bae, Hyoung-Churl; Renchinkhand, Gereltuya; Nam, Myoung-Soo;
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 Abstract
Lactobacillus salivarius subsp. salivarius Nam27 with a high -galactosidase activity was selected for enzymatic characterization. For purification, cell pellet was disrupted by Bead Beater, by DEAE-Sepharose and Mono-Q chromatography. The specific activity of the purified enzyme was 5,312 units/mg. The molecular weight of native monomeric -galactosidase was estimated to be 30,000 dalton (monomer) by the SDS-PAGE. The optimum temperature and optimum pH were and 5.0, respectively. This enzyme was stable between 35 and . -galactosidase activity was lost rapidly above pH 7.0. But -galactosidase was more stable at pH 4.0 (acidic conditions). And -galactosidase activity was lost rapidly above after 10 min incubation. and metal ions enhanced -galactosidase activity by 164.09% and 127.37% while , and lowered -galactosidase activity by 58.29%,85.10% and 77.66% respectively. Other metal ions didn`t affect -galactosidase activity significantly.
 Keywords
Lactobacillus salivarius;-galactosidase;purification;enzyme;
 Language
English
 Cited by
1.
β-Galactosidase from Lactobacillus pentosus: Purification, characterization and formation of galacto-oligosaccharides, Biotechnology Journal, 2010, 5, 8, 838  crossref(new windwow)
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