Characterization and application of an acidophilic and thermostable beta-glucosidase from Thermofilum pendens
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Li, Dan | - |
dc.contributor.author | Li, Xiaolei | - |
dc.contributor.author | Dang, Wei | - |
dc.contributor.author | Phuong Lan Tran | - |
dc.contributor.author | Park, Sung-Hoon | - |
dc.contributor.author | Oh, Byung-Chul | - |
dc.contributor.author | Hong, Wan-Soo | - |
dc.contributor.author | Lee, Jin-Sil | - |
dc.contributor.author | Park, Kwan-Hwa | - |
dc.date.available | 2020-02-28T23:47:49Z | - |
dc.date.created | 2020-02-06 | - |
dc.date.issued | 2013-05 | - |
dc.identifier.issn | 1389-1723 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/14597 | - |
dc.description.abstract | The gene encoding a beta-glucosidase from the archaeon Thermofilum pendens (Tpbgl) was cloned and expressed in Escherichia coli. The purified recombinant enzyme had a molecular mass of 77.8 kDa and released glucose or mannose from p-nitrophenyl-beta-D-glucopyra (pNPG), cellobiose, mannobiose, and genistin. Peak Tpbgl activity was detected at 90 degrees C, and 50% activity remained after incubation for 60 min at 95 degrees C. The optimal pH for pNPG hydrolysis was 3.5. When the enzyme was incubated with pNPG in the presence of ethanol and propanol, the glucose moiety was transferred to acceptor alcohols. Tpbgl is the archaeal beta-glucosidase from glucoside hydrolase family 3 and found to be most heat stable under extremely acidic conditions (pH 3.5). The kinetic parameters revealed that Tpbgl had the highest catalytic efficiency toward pNPG (k(cat)/K-m = 3.05) with strong substrate affinity for such natural substrates as cellobiose (K-m = 0.149) and mannobiose (K-m = 0.147). Genistin solubilized in 10-40% DMSO was hydrolyzed to genistein with nearly 99% conversion, indicating that high concentrations of the water-insoluble isoflavone glycoside can be treated by the enzyme. Our results indicate that Tpbgl has great potential in cellulose saccharification and the glucoside hydrolysis of natural compounds. (c) 2012, The Society for Biotechnology, Japan. All rights reserved. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | SOC BIOSCIENCE BIOENGINEERING JAPAN | - |
dc.relation.isPartOf | JOURNAL OF BIOSCIENCE AND BIOENGINEERING | - |
dc.subject | ARCHAEON PYROCOCCUS-FURIOSUS | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | SULFOLOBUS-SOLFATARICUS | - |
dc.subject | THERMOTOGA-NEAPOLITANA | - |
dc.subject | SUBSTRATE-SPECIFICITY | - |
dc.subject | TRANSGLYCOSYLATION ACTIVITY | - |
dc.subject | GENOME SEQUENCE | - |
dc.subject | BGLB GENE | - |
dc.subject | GLYCOSIDASE | - |
dc.subject | HYDROLASE | - |
dc.title | Characterization and application of an acidophilic and thermostable beta-glucosidase from Thermofilum pendens | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000320208600005 | - |
dc.identifier.doi | 10.1016/j.jbiosc.2012.11.009 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOSCIENCE AND BIOENGINEERING, v.115, no.5, pp.490 - 496 | - |
dc.identifier.scopusid | 2-s2.0-84876321656 | - |
dc.citation.endPage | 496 | - |
dc.citation.startPage | 490 | - |
dc.citation.title | JOURNAL OF BIOSCIENCE AND BIOENGINEERING | - |
dc.citation.volume | 115 | - |
dc.citation.number | 5 | - |
dc.contributor.affiliatedAuthor | Oh, Byung-Chul | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | beta-Glucosidase | - |
dc.subject.keywordAuthor | Thermofilum pendens | - |
dc.subject.keywordAuthor | Cellulose | - |
dc.subject.keywordAuthor | Glucoside | - |
dc.subject.keywordAuthor | Archaeon | - |
dc.subject.keywordPlus | ARCHAEON PYROCOCCUS-FURIOSUS | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | SULFOLOBUS-SOLFATARICUS | - |
dc.subject.keywordPlus | THERMOTOGA-NEAPOLITANA | - |
dc.subject.keywordPlus | SUBSTRATE-SPECIFICITY | - |
dc.subject.keywordPlus | TRANSGLYCOSYLATION ACTIVITY | - |
dc.subject.keywordPlus | GENOME SEQUENCE | - |
dc.subject.keywordPlus | BGLB GENE | - |
dc.subject.keywordPlus | GLYCOSIDASE | - |
dc.subject.keywordPlus | HYDROLASE | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Food Science & Technology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Food Science & Technology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
1342, Seongnam-daero, Sujeong-gu, Seongnam-si, Gyeonggi-do, Republic of Korea(13120)031-750-5114
COPYRIGHT 2020 Gachon University All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.