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One-step purification and characterization of a beta-1,4-glucosidase from a newly isolated strain of Stereum hirsutum

Authors
 Ngoc-Phuong-Thao Nguyen  ;  Kyoung-Mi Lee  ;  Kyoung-Min Lee  ;  In-Won Kim  ;  Yeong-Suk Kim  ;  Marimuthu Jeya  ;  Jung-Kul Lee 
Citation
 APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, Vol.87(6) : 2107-2116, 2010 
Journal Title
 APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 
ISSN
 0175-7598 
Issue Date
2010
MeSH
Basidiomycota/chemistry ; Basidiomycota/classification ; Basidiomycota/enzymology* ; Basidiomycota/isolation & purification* ; Enzyme Stability ; Fungal Proteins/chemistry* ; Fungal Proteins/genetics ; Fungal Proteins/isolation & purification* ; Fungal Proteins/metabolism ; Kinetics ; Molecular Sequence Data ; Molecular Weight ; Phylogeny ; Soil Microbiology* ; beta-Glucosidase/chemistry* ; beta-Glucosidase/genetics ; beta-Glucosidase/isolation & purification* ; beta-Glucosidase/metabolism
Keywords
β-1 ; 4-Glucosidase ; Glycoside hydrolase family 1 ; Glucoside ; Stereum hirsutum ; Wine fermentation
Abstract
A highly efficient beta-1,4-glucosidase (BGL) secreting strain, Stereum hirsutum SKU512, was isolated and identified based on morphological features and sequence analysis of internal transcribed spacer rDNA. A BGL containing a carbohydrate moiety was purified to homogeneity from S. hirsutum culture supernatants using only a single chromatography step on a gel filtration column. The relative molecular weight of S. hirsutum BGL was determined as 98 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis or 780 kDa by size exclusion chromatography, indicating that the enzyme is an octamer. S. hirsutum BGL showed the highest activity toward p-nitrophenyl-beta-D-glucopyranoside (V (max) = 3,028 U mg-protein(-1), k (cat) = 4,945 s(-1)) ever reported. The enzyme also showed good stability at an acidic pH ranging from 3.0 to 5.5. The BGL was able to promote transglycosylation with an activity of 42.9 U mg-protein(-1) using methanol as an acceptor and glucose as a donor. The internal amino acid sequences of the isolated enzyme showed significant homology with hydrolases from glycoside hydrolase family 1 (GH1), indicating that the S. hirsutum BGL is a member of GH1 family. The characteristics of S. hirsutum BGL could prove to be of interest in several potential applications, especially in enhancing flavor release during the wine fermentation process.
Full Text
https://link.springer.com/article/10.1007/s00253-010-2668-2
DOI
10.1007/s00253-010-2668-2
Appears in Collections:
1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
Yonsei Authors
Lee, Kyoung Mi(이경미) ORCID logo https://orcid.org/0000-0002-9038-8162
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/158128
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