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KMID : 0613820080180060845
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Journal of Life Science
2008 Volume.18 No. 6 p.845 ~ p.851
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Purification and Characterization of β-Lactamase Secreted from Bacillus sp. J105 Strain having β-Lactam Antibiotics Resistance
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Cho Kyung-Soon
Kang Byoung-Won
Seo Min-Jeong
Lee Young-Chun
Lee Jai-Heon
Joo Woo-Hong
Choi Yung-Hyun
Lim Hak-Seob
Kim Jung-In
Seo Kwon-Il
Jeong Yong-Kee
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Abstract
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β-Lactamase, secreted from Bacillus sp. J105 strain was purified to a single band on SDS-PAGE by ammonium sulfate precipitation, ion exchange column chromatography and gel-filtration. The molecular weight of the purified enzyme was 31 kDa on SDS-PAGE and its isoelectric point was 7.35. Optimal pH and temperature for enzymatic reaction were 5 and 40℃, respectively. As a result of total amino acid composition analysis of the purified enzyme, Gly and Ala were occupied 14.1 and 13.3 mole %, respectively. Km and Vmax value of purified enzyme were 1.33 mM and 0.36 mM/㎖ using ampicillin as a substrate, respectively.
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KEYWORD
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Antibiotics, Bacillussp.J105, β-lactamase, β-lactam, enzymepurification
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