Purification and characterization of Clostridium thermocellum xylanase from recombinant Escherichia coli

Cited 0 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorBon Joon Koo-
dc.contributor.authorHwa Gyun Oh-
dc.contributor.authorKi Haeng Cho-
dc.contributor.authorChang Kun Yang-
dc.contributor.authorKyung Hwa Jung-
dc.contributor.authorDai Young Ryu-
dc.date.accessioned2017-04-19T08:57:45Z-
dc.date.available2017-04-19T08:57:45Z-
dc.date.issued1996-
dc.identifier.issn1017-7825-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5372-
dc.description.abstractThe xylnX gene encoding a xylanase from Clostridium thermocellum ATCC27405 was cloned in the plasmid pJH27, an E. coli-Bacillus shuttle vector and the resultant recombinant plasmid, pJX18 was transformed into E. coli HB101. The overexpressed xylanase was found to be secreted into the periplasmic space of the recombinant E. coli cells. The crude enzyme was obtained by treating the E. coli cells with lysozyme, and purified by DEAE-Sepharose column chromatography. Molecular wieght of the xylanase was estimated to be 53 kDa by gel filtration. The pI value was determined to be pH 8.8. The N-terminal sequence of the enzyme protein was Asp-Asp-Asn-Asn-Ala-Asn-Leu-Val-Ser-Asn which was considered to be the sequence of that of the mature form protein. The Km value of the enzyme for oat spelt xylan was calculated to be 2.63 mg/ml and the Vmax value was 0.47 μmole/min. The xylanase had a pH optimum for its activity at pH 5.4 and a temperature optimum at 60°C. The enzyme hydrolyzed xylan into xylooligosaccharides which were composed mainly of xylobiose (40%) and xyloltriose (12%) after 5 hour reaction. This result indicates that the xylanase from C. thermocellum ATCC27405 is an endo-acting enzyme.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titlePurification and characterization of Clostridium thermocellum xylanase from recombinant Escherichia coli-
dc.title.alternativePurification and characterization of Clostridium thermocellum xylanase from recombinant Escherichia coli-
dc.typeArticle-
dc.citation.titleJournal of Microbiology and Biotechnology-
dc.citation.number6-
dc.citation.endPage419-
dc.citation.startPage414-
dc.citation.volume6-
dc.contributor.affiliatedAuthorKyung Hwa Jung-
dc.contributor.alternativeName구본준-
dc.contributor.alternativeName오화균-
dc.contributor.alternativeName조기행-
dc.contributor.alternativeName양창근-
dc.contributor.alternativeName정경화-
dc.contributor.alternativeName류대영-
dc.identifier.bibliographicCitationJournal of Microbiology and Biotechnology, vol. 6, no. 6, pp. 414-419-
dc.subject.keywordclostridium thermocellum-
dc.subject.keywordxylanase-
dc.subject.localClostridium thermocellum-
dc.subject.localclostridium thermocellum-
dc.subject.localXylanase-
dc.subject.localxylanase-
dc.description.journalClassY-
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


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