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KMID : 1024620070270010102
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Food Science of Animal Resources
2007 Volume.27 No. 1 p.102 ~ p.109
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Purification and Characterization of -Galactosidase from Lactobacillus salivarius subsp. salivarius Nam27
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Bae Hyoung-Cchurl
Choi Jong-Woo
Nam Myoung-Soo
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Abstract
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Lactobacillus salivarius subsp. salivarius CNU27 possessed a high level of -galactosidase activity. Purified -galactosidase was obtained after sonication of harvested cell pellet followed by DEAE-Sephadex A-50 and Mono Q anion exchange chromatography. The specific activity of the purified enzyme was 8,994 units/mg protein which is 17.09 times higher than that in crude extract. The native enzyme was a monomer with a molecular mass of 56,397.1 dalton. The optimum temperature and pH for the enzyme were and 6.0, respectively. The enzyme was stable between 25 and . However, -galactosidase activity was lost rapidly below pH 4.5 and above pH 8.5. The enzyme activity decreased to 6.73% and 4.30% of the original activity by addition of and , respectively. Other metal compounds did not affect the enzyme activity significantly. The enzyme liberated galactose from melibiose, raffinose, and stachyose. The rate of substrates hydrolysis was measured by HPLC. Raffinose, stachyose and melibiose were completely decomposed after 24 hr at .
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KEYWORD
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Lactobacillus salivarius, -galactosidase, purification, enzyme
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