Biochemical characterization of two xylanases from yeast Pseudozyma hubeiensis producing only xylooligosaccharides

TitleBiochemical characterization of two xylanases from yeast Pseudozyma hubeiensis producing only xylooligosaccharides
Publication TypeJournal Article
Year of Publication2009
AuthorsAdsul, MG, Bastawade, KB, Gokhale, DV
JournalBioresource Technology
Volume100
Issue24
Pagination6488-6495
Date PublishedDEC
ISSN0960-8524
KeywordsCellulase-free xylanase, Pseudozyma hubeiensis, Xylooligosaccharides
Abstract

Two distinct xylanases from Pseudozyma hubeiensis NCIM 3574 were purified to homogeneity. The molecular masses of two native xylanases were 33.3 kDa (PhX33) and 20.1 kDa (PhX20). PhX33 is predominant with alpha-helix and PhX20 contained predominantly beta-sheets. Xylanase, PhX33, possesses three tryptophan and one carboxyl residues at the active site. The active site of PhX20 comprises one residue each of tryptophan, carboxyl and histidine. Carboxyl residue is mainly involved in catalysis and tryptophane residues are solely involved in substrate binding. Histidine residue present at the active site of PhX20 appeared to have a role in substrate binding. Both the xylanases produced only xylooligosaccharides (XOS) with degree of polymerization (DP) 3-7 without formation of xylose and xylobiose. These XOS could be used in functional foods or as prebiotics. Lc ms-ms ion search of cryptic digestion of these xylanases revealed that there is no significant homology of peptides with known fungal xylanase sequences which indicate that these xylanases appear to be new. (c) 2009 Elsevier Ltd. All rights reserved.

DOI10.1016/j.biortech.2009.07.064
Type of Journal (Indian or Foreign)Foreign
Impact Factor (IF)4.365
Divison category: 
National Collection of Industrial Micr-organisms (NCIM)