A Novel Glycosyl Hydrolase Family 16 beta-Agarase from the Agar-Utilizing Marine Bacterium Gilvimarinus agarilyticus JEA5: the First Molecular and Biochemical Characterization of Agarase in Genus Gilvimarinus SCIE SCOPUS KCI

DC Field Value Language
dc.contributor.author Lee, Youngdeuk -
dc.contributor.author Jo, Eunyoung -
dc.contributor.author Lee, Yeon-Ju -
dc.contributor.author Hettiarachchi, Sachithra Amarin -
dc.contributor.author Park, Gun-Hoo -
dc.contributor.author Lee, Su-Jin -
dc.contributor.author Heo, Soo-Jin -
dc.contributor.author Kang, Do-Hyung -
dc.contributor.author Oh, Chulhong -
dc.date.accessioned 2020-04-16T08:55:17Z -
dc.date.available 2020-04-16T08:55:17Z -
dc.date.created 2020-01-28 -
dc.date.issued 2018-05 -
dc.identifier.issn 1017-7825 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/926 -
dc.description.abstract The agarase gene gaa16a was identified from a draft genome sequence of Gilvimarinus agarilyticus JEA5, an agar-utilizing marine bacterium. Recently, three agarase-producing bacteria, G. chinensis, G. polysaccharolyticus, and G. agarilyticus, in the genus Gilvimarinus were reported. However, there have been no reports of the molecular characteristics and biochemical properties of these agarases. In this study, we analyzed the molecular characteristics and biochemical properties of agarases in Gilvimarinus. Gaa16A comprised a 1,323-bp open reading frame encoding 441 amino acids. The predicted molecular mass and isoelectric point were 49 kDa and 4.9, respectively. The amino acid sequence of Gaa16A showed features typical of glycosyl hydrolase family 16 (GH16) beta-agarases, including a GH16 domain, carbohydrate-binding region (RICIN domain), and signal peptide. Recombinant Gaa16A (excluding the signal peptide and carbohydrate-binding region, rGaa16A) was expressed as a fused protein with maltose-binding protein at its N-terminus in Escherichia coli. rGaa16A had maximum activity at 55 degrees C and pH 7.0 and 103 U/mg of specific activity in the presence of 2.5 mM CaCl2 . The enzyme hydrolyzed agarose to yield neoagarotetraose as the main product. This enzyme may be useful for industrial production of functional neoagaro-oligosaccharides. -
dc.description.uri 1 -
dc.language English -
dc.subject PURIFICATION -
dc.subject CLONING -
dc.subject EXPRESSION -
dc.subject GALACTOSE -
dc.subject GENOME -
dc.subject ENZYME -
dc.subject SP. -
dc.title A Novel Glycosyl Hydrolase Family 16 beta-Agarase from the Agar-Utilizing Marine Bacterium Gilvimarinus agarilyticus JEA5: the First Molecular and Biochemical Characterization of Agarase in Genus Gilvimarinus -
dc.type Article -
dc.citation.endPage 783 -
dc.citation.startPage 776 -
dc.citation.volume 28 -
dc.citation.number 5 -
dc.identifier.bibliographicCitation JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.28, no.5, pp.776 - 783 -
dc.identifier.doi 10.4014/jmb.1709.09050 -
dc.identifier.scopusid 2-s2.0-85047788859 -
dc.identifier.wosid 000433224400013 -
dc.type.docType Article -
dc.identifier.kciid ART002348320 -
dc.description.journalClass 1 -
dc.subject.keywordPlus PURIFICATION -
dc.subject.keywordPlus CLONING -
dc.subject.keywordPlus EXPRESSION -
dc.subject.keywordPlus POLYSACCHARIDE -
dc.subject.keywordPlus GALACTOSE -
dc.subject.keywordPlus GENOME -
dc.subject.keywordPlus ENZYME -
dc.subject.keywordPlus SP. -
dc.subject.keywordAuthor Gilvimarinus -
dc.subject.keywordAuthor agarase -
dc.subject.keywordAuthor neoagaro-oligosaccharides -
dc.subject.keywordAuthor cloning -
dc.subject.keywordAuthor overexpression -
dc.relation.journalWebOfScienceCategory Biotechnology & Applied Microbiology -
dc.relation.journalWebOfScienceCategory Microbiology -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.description.journalRegisteredClass kci -
dc.relation.journalResearchArea Biotechnology & Applied Microbiology -
dc.relation.journalResearchArea Microbiology -
Appears in Collections:
Jeju Research Institute > Jeju Marine Research Center > 1. Journal Articles
Marine Resources Research Division > Marine Biotechnology Research Center > 1. Journal Articles
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