Title of article :
Functional characterization and synergic action of fungal xylanase and arabinofuranosidase for production of xylooligosaccharides
Author/Authors :
Gonçalves، نويسنده , , T.A. and Damلsio، نويسنده , , A.R.L. and Segato، نويسنده , , F. and Alvarez، نويسنده , , T.M. and Bragatto، نويسنده , , J. and Brenelli، نويسنده , , L.B. and Citadini، نويسنده , , A.P.S. and Murakami، نويسنده , , M.T. and Ruller، نويسنده , , R. and Paes Leme، نويسنده , , A.F. and Prade، نويسنده , , R.A. and Squina، نويسنده , , F.M.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2012
Pages :
7
From page :
293
To page :
299
Abstract :
Plant cell wall degrading enzymes are key technological components in biomass bioconversion platforms for lignocellulosic materials transformation. Cost effective production of enzymes and identification of efficient degradation routes are two economic bottlenecks that currently limit the use of renewable feedstocks through an environmental friendly pathway. The present study describes the hypersecretion of an endo-xylanase (GH11) and an arabinofuranosidase (GH54) by a fungal expression system with potential biotechnological application, along with comprehensive characterization of both enzymes, including spectrometric analysis of thermal denaturation, biochemical characterization and mode of action description. The synergistic effect of these enzymes on natural substrates such as sugarcane bagasse, demonstrated the biotechnological potential of using GH11 and GH54 for production of probiotic xylooligosaccharides from plant biomass. Our findings shed light on enzymatic mechanisms for xylooligosaccharide production, as well as provide basis for further studies for the development of novel enzymatic routes for use in biomass-to-bioethanol applications.
Keywords :
Hemicellulosic feedstock , Sugar cane bagasse , xylooligosaccharides , Endo-xylanases , Arabinofuranosidases
Journal title :
Bioresource Technology
Serial Year :
2012
Journal title :
Bioresource Technology
Record number :
1929477
Link To Document :
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