Characterization of a Thermostable β-glucosidase from the Hyperthermophilic Archaeon Thermococcus pacificus

DC Field Value Language
dc.contributor.author 이재은 -
dc.contributor.author 김윤재 -
dc.contributor.author 이현숙 -
dc.contributor.author 강성균 -
dc.contributor.author 이정현 -
dc.contributor.author 권개경 -
dc.date.accessioned 2020-07-16T04:52:14Z -
dc.date.available 2020-07-16T04:52:14Z -
dc.date.created 2020-02-11 -
dc.date.issued 2014-05-02 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/26295 -
dc.description.abstract Hyperthermophilc archaeon, Thermococcus pacificus (Topt of 80-88 °C) could grow on various substrates such as peptides, starch, and so on. Based on the genomic analysis of the strain, we identified a novel GH1 β-glucosidase encoding gene (PAC_orf01364), which was located in glycoside hydrolase gene clusters consisting of cellulose-, laminarin-, and agarose-degrading enzymes. The gene revealed an ORF of 1,464 bp encoding 487 amino acid residues, and the deduced amino acid sequence showed 77% identity with Pyrococcus furiosus β-glucosidase (accession no. NP_577802). The gene was cloned and expressed in Escherchia coli system. The recombinant protein was purified by metal affinity chromatography and characterized. The purified enzyme shows optimum activity at pH 5.5 and 75 °C, and thermostability with a half life of 6 h at 90 °C. Interestingly, the enzyme also exhibits laminarinase activity and β-xylosidase activity.(PAC_orf01364), which was located in glycoside hydrolase gene clusters consisting of cellulose-, laminarin-, and agarose-degrading enzymes. The gene revealed an ORF of 1,464 bp encoding 487 amino acid residues, and the deduced amino acid sequence showed 77% identity with Pyrococcus furiosus β-glucosidase (accession no. NP_577802). The gene was cloned and expressed in Escherchia coli system. The recombinant protein was purified by metal affinity chromatography and characterized. The purified enzyme shows optimum activity at pH 5.5 and 75 °C, and thermostability with a half life of 6 h at 90 °C. Interestingly, the enzyme also exhibits laminarinase activity and β-xylosidase activity. -
dc.description.uri 2 -
dc.language English -
dc.publisher 한국미생물학회 -
dc.relation.isPartOf 한국미생물학회 춘계 학술대회 -
dc.title Characterization of a Thermostable β-glucosidase from the Hyperthermophilic Archaeon Thermococcus pacificus -
dc.type Conference -
dc.citation.conferencePlace KO -
dc.citation.endPage 252 -
dc.citation.startPage 252 -
dc.citation.title 한국미생물학회 춘계 학술대회 -
dc.identifier.bibliographicCitation 한국미생물학회 춘계 학술대회, pp.252 -
dc.description.journalClass 2 -
Appears in Collections:
Marine Resources Research Division > Marine Biotechnology Research Center > 2. Conference Papers
Files in This Item:
There are no files associated with this item.

qrcode

Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse