Purification and characterization of thermostable beta-glucosidase from the brown-rot basidiomycete Fomitopsis palustris grown on microcrystalline cellulose
- Authors
- Yoon, Jeong-Jun; Kim, Ki-Yeon; Cha, Chang-Jun
- Issue Date
- Feb-2008
- Publisher
- MICROBIOLOGICAL SOCIETY KOREA
- Keywords
- beta-glucosidase; brown-rot fungus; Fomitopsis palustris; purification; microcrystalline cellulose
- Citation
- JOURNAL OF MICROBIOLOGY, v.46, no.1, pp 51 - 55
- Pages
- 5
- Journal Title
- JOURNAL OF MICROBIOLOGY
- Volume
- 46
- Number
- 1
- Start Page
- 51
- End Page
- 55
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/23853
- DOI
- 10.1007/s12275-007-0230-4
- ISSN
- 1225-8873
1976-3794
- Abstract
- An extracellular beta-glucosidase was purified 154-fold to electrophoretic homogeneity from the brown-rot basidiomycete Fomitopsis palustris grown on 2.0% microcrystalline cellulose. SDS-polyacrylamide gel electrophoresis gel gave a single protein band and the molecular mass of purified enzyme was estimated to be approximately 138 kDa. The amino acid sequences of the proteolytic fragments determined by nano-LC-MS/MS suggested that the protein has high homology with fungal beta-glucosidases that belong to glycosyl hydrolase family 3. The K(m)s for p-nitorophenyl-beta-D-glucoside (p-NPG) and cellobiose hydrolyses were 0.117 and 4.81 mM, and the K-cat values were 721 and 101.8 per see, respectively. The enzyme was competitively inhibited by both glucose (K-i= 0.35 mM) and gluconolactone (K-i= 0.008 mM), when p-NPG was used as substrate. The optimal activity of the purified beta-glucosidase was observed at pH 4.5 and 70 degrees C. The F. palustris protein exhibited half-lives of 97 h at 55 degrees C and 15 h at 65 degrees C, indicating some degree of thermostability. The enzyme has high activity against p-NPG and cellobiose but has very little or no activity against p-nitrophenyl-beta-lactoside, p-nitrophenyl-beta-xyloside, p-nitrophenyl-alpha-arabinofuranoside, xylan, and carboxymethyl cellulose. Thus, our results revealed that the beta-glucosidase from F. palustris can be classified as an aryl-beta-glucosidase with cellobiase activity.
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Collections - College of Biotechnology & Natural Resource > Department of Systems Biotechnology > 1. Journal Articles
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