Purification and Characterization of an Extracellular beta-Glucosidase Produced by Phoma sp KCTC11825BP Isolated from Rotten Mandarin Peel
- Authors
- Choi, Jung-Youn; Park, Ah-Reum; Kim, Yong Jin; Kim, Jae-Jin; Cha, Chang-Jun; Yoon, Jeong-Jun
- Issue Date
- 5월-2011
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Phoma sp.; beta-glucosidase; identification; purification; characterization
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.21, no.5, pp.503 - 508
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 21
- Number
- 5
- Start Page
- 503
- End Page
- 508
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/112555
- DOI
- 10.4014/jmb.1102.02014
- ISSN
- 1017-7825
- Abstract
- A beta-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 beta-glucosidase evidenced high homology with the fungal beta-glucosidases belonging to glycosyl hydrolase family 3. Its optimal activity was detected at pH 4.5 and 60 degrees C, and the enzyme had a half-life of 53 h at 60 degrees C. The K-m for p-nitrophenyl-beta-D-glucopyranoside and cellobiose were 0.3 mM and 3.2 mM, respectively. The enzyme was competitively inhibited by both glucose (K-i=1.7 mM) and glucono-delta-lactone (K-i=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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Collections - College of Life Sciences and Biotechnology > Division of Environmental Science and Ecological Engineering > 1. Journal Articles
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