Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/14447
ชื่อเรื่อง: Purification, characterization and gene cloning of two forms of a thermostable endo-xylanase from Streptomyces sp. SWU10
ผู้แต่ง: Deesukon W.
Nishimura Y.
Harada N.
Sakamoto T.
Sukhumsirichart W.
Keywords: Amino acid residues
Amino acid sequence
Birch wood
Coding sequences
Culture filtrate
Endoxylanase
Gene cloning
Glycoside hydrolases
In-vitro
Initial activity
Optimal temperature
Potential applications
Proteolytic fragments
Rice straws
Side-chains
Streptomyces coelicolor A3(2)
Streptomyces sp
Streptomyces sp., Endo-xylanases, Characterization, Gene cloning, Glycosyl hydrolase family 10
Time of flight
Wide pH range
Xylanases
Amino acids
Bacteria
Cloning
Encoding (symbols)
Hydrolases
Mass spectrometry
Sugars
Textile industry
Textile processing
Waste treatment
Gene encoding
Streptomyces
Streptomyces coelicolor
Streptomyces sp.
วันที่เผยแพร่: 2011
บทคัดย่อ: Two forms of an endo-xylanase were isolated from the culture filtrate of Streptomyces sp. SWU10 that grew on rice straw. The molecular masses of both forms of an enzyme were 31 kDa (XynSW2A) and 44 kDa (XynSW2B). Analysis of internal amino acid sequences of the proteins by liquid chromatography/ion-trap/ time-of flight mass spectrometer (LC/IT/TOF MS) revealed that XynSW2A may be the proteolytic fragment of XynSW2B. Optimal temperature and pH of XynSW2A and XynSW2B were 60 °C and 6.0, respectively. Both forms of the enzyme were stable in a wide pH ranges. More than 80% of the initial activities remained at pH 3-9 (XynSW2A) and 2-9 (XynSW2B) after 16 h of incubation at 4 °C. XynSW2A and XynSW2B were stable up to 80 °C and 60 °C, respectively. Both forms of the enzyme were strongly inhibited by Hg2+ ions. Birch wood xylan, which has no arabinofuranosyl side chains, was the most preferred substrate for both forms. The xynSW2 gene encoding XynSW2B was isolated by in vitro cloning. The coding sequence of xynSW2 gene was 1434 bp in length and encode a polypeptide of 477 amino acid residues. Pfam analysis revealed Glycohydro 10 and Ricinβlectin domains in XynSW2B. The deduced amino acid sequence of XynSW2B exhibited the highest identity with that of a xylanase A of Streptomyces coelicolor A3(2) belong to glycoside hydrolase (GH) family 10. Because of their pH and thermal stabilities, XynSW2A and XynSW2B may have potential application in biofuel industry by using rice straw and can be applied in food, textile industries, and waste treatment. © 2011 Elsevier Ltd. All rights reserved.
URI: https://ir.swu.ac.th/jspui/handle/123456789/14447
https://www.scopus.com/inward/record.uri?eid=2-s2.0-80055000471&doi=10.1016%2fj.procbio.2011.09.004&partnerID=40&md5=f5db7c156a94c0034f37c2b17c410b95
ISSN: 13595113
Appears in Collections:Scopus 1983-2021

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