alexa Properties of β-Galactosidase from Lactobacillus salivarius subsp. salivarius Nam27


Journal of Food & Industrial Microbiology

Author(s): HyoungChurl Bae, Gereltuya Renchinkhand, MyoungSoo Nam

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Lactobacillus salivarius subsp. salivarius Nam27 with a high β-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 β-galactosidase was estimated to be 30,000 dalton (monomer) by the SDS-PAGE. The optimum temperature and optimum pH were 50°C and 5.0, respectively. This enzyme was stable between 35 and 55°C. β-Galactosidase activity was lost rapidly above pH 7.0. But β-galactosidase was more stable at pH 4.0 (acidic conditions). And β-galactosidase activity was lost rapidly above 65°C after 10 min incubation. Ca2+ and Zn2+ metal ions enhanced β-galactosidase activity by 164.09% and 127.37%, while Cu2+, Fe3+ and Mn2+ lowered β-galactosidase activity by 58.29%, 85.10% and 77.66%, respectively. Other metal ions didn't affect β-galactosidase activity significantly.

This article was published in Korean journal for food science of animal resources and referenced in Journal of Food & Industrial Microbiology

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