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.
journal_name
Appl Biochem Biotechnoljournal_title
Applied biochemistry and biotechnologyauthors
Kui H,Luo H,Shi P,Bai Y,Yuan T,Wang Y,Yang P,Dong S,Yao Bdoi
10.1007/s12010-009-8815-5subject
Has Abstractpub_date
2010-10-01 00:00:00pages
953-65issue
4eissn
0273-2289issn
1559-0291journal_volume
162pub_type
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