نتایج جستجو برای: xylanases

تعداد نتایج: 710  

Journal: :Journal of molecular biology 2000
M D Joshi G Sidhu I Pot G D Brayer S G Withers L P McIntosh

The pH optima of family 11 xylanases are well correlated with the nature of the residue adjacent to the acid/base catalyst. In xylanases that function optimally under acidic conditions, this residue is aspartic acid, whereas it is asparagine in those that function under more alkaline conditions. Previous studies of wild-type (WT) Bacillus circulans xylanase (BCX), with an asparagine residue at ...

Journal: :Vietnam Journal of Science and Technology 2021

Abstract. The multifunctional GH78 glycoside hydrolase from the soft rot ascomycete Xylaria polymorpha (XpoGH78) catalyzed conversion of different lignocellulosic materials to release carbohydrates and biomethanol. disintegrating effect enzymatic lignocellulose treatment can be significantly improved by using kinds hydrolases a phenol oxidase. Thus, rape straw meal XpoGH78 could optimized in pr...

Journal: :Journal of bacteriology 2015
Magali Solé Felix Scheibner Anne-Katrin Hoffmeister Nadine Hartmann Gerd Hause Annekatrin Rother Michael Jordan Martine Lautier Matthieu Arlat Daniela Büttner

UNLABELLED Many plant-pathogenic bacteria utilize type II secretion (T2S) systems to secrete degradative enzymes into the extracellular milieu. T2S substrates presumably mediate the degradation of plant cell wall components during the host-pathogen interaction and thus promote bacterial virulence. Previously, the Xps-T2S system from Xanthomonas campestris pv. vesicatoria was shown to contribute...

Journal: :Biocatalysis and Biotransformation 2021

The biochemical conversion route in the utilization of biomass has required intensive development processing methods for reducing recalcitrance cellulose to enzymatic hydrolysis. Since discovering hydrophilic ionic liquids (ILs) are efficient lignocellulose solvents, considerable efforts have been made demonstrate their potential applications However, most commercial hydrolyzing enzymes largely...

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