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Biochemical and molecular characterization of a cellobiohydrolase from Trametes versicolor.

Author(s): Lahjouji K, Storms R, Xiao Z, Joung KB, Zheng Y, Powlowski J, Tsang A, Varin L

Appl Microbiol Biotechnol. 2007 May;75(2):337-46 Authors: Lahjouji K, Storms R, Xiao Z, Joung KB, Zheng Y, Powlowski J, Tsang A, Varin L

Article GUID: 17333176
Development of a pyrG mutant of Aspergillus oryzae strain S1 as a host for the production of heterologous proteins.

Author(s): Ling SO, Storms R, Zheng Y, Rodzi MR, Mahadi NM, Illias RM, Abdul Murad AM, Abu Bakar FD

ScientificWorldJournal. 2013;2013:634317 Authors: Ling SO, Storms R, Zheng Y, Rodzi MR, Mahadi NM, Illias RM, Abdul Murad AM, Abu Bakar FD

Article GUID: 24381522
Enhancement of synthetic Trichoderma-based enzyme mixtures for biomass conversion with an alternative family 5 glycosyl hydrolase from Sporotrichum thermophile.

Author(s): Ye Z, Zheng Y, Li B, Borrusch MS, Storms R, Walton JD

PLoS One. 2014;9(10):e109885 Authors: Ye Z, Zheng Y, Li B, Borrusch MS, Storms R, Walton JD

Article GUID: 25295862
Title:Biochemical and molecular characterization of a cellobiohydrolase from Trametes versicolor.
Authors:Lahjouji K,  Storms R,  Xiao Z,  Joung KB,  Zheng Y,  Powlowski J,  Tsang A,  Varin L
Link:https://www.ncbi.nlm.nih.gov/pubmed/17333176?dopt=Abstract
DOI:10.1007/s00253-006-0824-5
Category:Appl Microbiol Biotechnol
PMID:17333176
Dept Affiliation: BIOLOGY
1 Centre for Structural and Functional Genomics, Biology Department, Concordia University, 7141 Sherbrooke street West, Montréal, Quebec, H4B 1R6, Canada.

Description:

Biochemical and molecular characterization of a cellobiohydrolase from Trametes versicolor.

Appl Microbiol Biotechnol. 2007 May;75(2):337-46

Authors: Lahjouji K, Storms R, Xiao Z, Joung KB, Zheng Y, Powlowski J, Tsang A, Varin L

Abstract

A cellobiohydrolase-encoding cDNA, Tvcel7a, from Trametes versicolor has been cloned and expressed in Aspergillus niger. The deduced amino acid sequence shows that Tvcel7a encodes a 456-amino acid polypeptide belonging to glycosyl hydrolase family 7. TvCel7a possesses a 19-amino acid secretion signal but does not possess a linker region nor a carbohydrate-binding domain. Two peaks of activity were obtained after TvCel7a was purified to apparent homogeneity by gel-filtration followed by anion-exchange chromatography. Mass spectrometry performed on the purified proteins confirmed that both peaks corresponded to the predicted sequence of the T. versicolor cellulase. The biochemical properties of the purified TvCel7a obtained from both peaks were studied in detail. The pH and temperature optima were 5.0 and 40 degrees C, respectively. The enzyme was stable over a pH range extending from pH 3.0 to 9.0 and at temperatures lower than 50 degrees C. The kinetic parameters with the substrate p-nitrophenyl beta-D: -cellobioside (pNPC) were 0.58 mM and 1.0 micromol/min/mg protein for the purified TvCel7a found in both peaks 1 and 2. TvCel7a catalyzes the hydrolysis of pNPC, filter paper, beta-glucan, and avicel to varying extents, but no detectable hydrolysis was observed when using the substrates carboxymethylcellulose, laminarin and pNPG.

PMID: 17333176 [PubMed - indexed for MEDLINE]