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Cloning and characterization of a xylanase, KRICT PX1 from the strain Paenibacillus sp. HPL-001

Paper ID Volume ID Publish Year Pages File Format Full-Text
14396 1216 2010 8 PDF Available
Title
Cloning and characterization of a xylanase, KRICT PX1 from the strain Paenibacillus sp. HPL-001
Abstract

The KRICT PX1 gene (GB: FJ380951) consisting of 996 bp encoding a protein of 332 amino acids (38.1 kDa) from the recently isolated Paenibacillus sp. strain HPL-001 (KCTC11365BP) has been cloned and expressed in Escherichia coli. The xylanase KRICT PX1 showed high activity on birchwood xylan, and was active over a pH range of 5.0 to 11.0, with two optima at pH 5.5 and 9.5 at 50 °C with Km value of 5.35 and 3.23, respectively. The xylanase activity was not affected by most salts, such as NaCl, LiCl, KCl, NH4Cl, CaCl2, MgCl2, MnCl2, and CsCl2 at 1 mM, but affected by CuSO4, ZnSO4, and FeCl3. One mM of EDTA, 2-mercaptoethanol, and PMSF did not affect the xylanase activity. TLC analysis of the catalyzed products after reaction with birchwood xylan revealed that xylobiose was the major product with smaller amounts of xylotriose and xylose. A similarity analysis of the amino acids in KRICT PX1 resulted 72% identity with xylanase from Geobacillus stearothermophilus (GB: ZP_03040360), 70% identity with intracellular xylanase from an uncultured bacterium (GB: AAP51133), 68% identity with endo-1-4-xylanse from Paenibacillus sp. (GB: ZP_02847150). In addition, the amino acid alignment of KRICT PX1 with glycosyl hydralase (GH) family 10 xylanases revealed a high degree of homology in highly conserved regions including the catalytic sites, and this was confirmed through PROSITE scan. These results imply that KRICT PX1 is a new xylanase gene, and this alkaline xylanase belongs to GH family 10.

Keywords
Paenibacillus sp. HPL-001; Xylanase; Characterization; Recombinant KRICT PX1
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Cloning and characterization of a xylanase, KRICT PX1 from the strain Paenibacillus sp. HPL-001
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biotechnology Advances - Volume 28, Issue 5, September–October 2010, Pages 594–601
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us