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KMID : 0545120110210050503
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Journal of Microbiology and Biotechnology
2011 Volume.21 No. 5 p.503 ~ p.508
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Purification and Characterization of an Extracellular β-Glucosidase Produced by Phoma sp. KCTC11825BP Isolated from Rotten Mandarin Peel
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Choi Jung-Youn
Park Ah-Reum
Kim Yong-Jin
Kim Jae-Jin
Cha Chang-Jun
Yoon Jeong-Jun
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Abstract
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A β-glucosidase from Phoma sp. KCTC11825BP isolated from rotten mandarin peel was purified 8.5-fold with a specific activity of 84.5 U/mg protein. The purified enzyme had a molecular mass of 440 kDa with a subunit of 110 kDa. The partial amino acid sequence of the purified β-glucosidase evidenced high homology with the fungal β- glucosidases belonging to glycosyl hydrolase family 3. Its optimal activity was detected at pH 4.5 and 60oC, and the enzyme had a half-life of 53 h at 60oC. The Km values for p-nitrophenyl-β-D-glucopyranoside and cellobiose were 0.3 mM and 3.2 mM, respectively. The enzyme was competitively inhibited by both glucose (Ki=1.7 mM) and glucono-δ-lactone (Ki=0.1 mM) when pNPG was used as the substrate. Its activity was inhibited by 41% by 10 mM Cu2+ and stimulated by 20% by 10 mM Mg2+.
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KEYWORD
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Phoma sp., β-glucosidase, Identification, Purification, Characterization
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