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  • Title: Gene cloning, expression, and characterization of a thermostable xylanase from Nesterenkonia xinjiangensis CCTCC AA001025.
    Author: Kui H, Luo H, Shi P, Bai Y, Yuan T, Wang Y, Yang P, Dong S, Yao B.
    Journal: Appl Biochem Biotechnol; 2010 Oct; 162(4):953-65. PubMed ID: 19838860.
    Abstract:
    An endo-beta-1,4-xylanase-encoding gene, xyn11NX, was cloned from Nesterenkonia xinjiangensis CCTCC AA001025 and expressed in Escherichia coli. The gene encoded a 192-amino acid polypeptide and a putative 50-amino acid signal peptide. The deduced amino acid sequence exhibited a high degree of similarity with the xylanases from Streptomyces thermocyaneoviolaceus (68%) and Thermobifida fusca (66%) belonging to glycoside hydrolase family 11. After purification to homogeneity, the recombinant Xyn11NX exhibited optimal activity at pH 7.0 and 55 degrees C and remained stable at weakly acidic to alkaline pH (pH 5.0-11.0). The enzyme was thermostable, retaining more than 80% of the initial activity after incubation at 60 degrees C for 1 h and more than 40% of the activity at 90 degrees C for 15 min. The K (m) and V (max) values for oat spelt xylan and birchwood xylan were 16.08 mg ml(-1) and 45.66 micromol min(-1) mg(-1) and 9.22 mg ml(-1) and 16.05 micromol min(-1) mg(-1), respectively. The predominant hydrolysis products were xylobiose and xylotriose when using oat spelt xylan or birchwood xylan as substrate.
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