Biomaterial Database

Specificity of an esterase (XYLD) from Pseudomonas fluorescens subsp. cellulosa. 1995

C B Faulds, and M C Ralet, and G Williamson, and G P Hazlewood, and H J Gilbert

Department of Food Molecular Biochemistry, Norwich Laboratory, UK.

Activity of an esterase from Pseudomonas fluorescens subsp. cellulosa (XYLD) on an insoluble feruloylated hemicellulose substrate (de-starched wheat bran) was dependent on the source of added endo-xylanase. The esterase exhibited high selectivity for the nature, position of linkage and size of the feruloylated oligosaccharides generated by hydrolysis of the hemicellulose. Increased affinity of XYLD with increasing size of the oligosaccharide substrate suggests that optimal activity is observed on substrates with at least 4 sugars.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D009844	Oligosaccharides	Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.	Oligosaccharide
D011551	Pseudomonas fluorescens	A species of nonpathogenic fluorescent bacteria found in feces, sewage, soil, and water, and which liquefy gelatin.	Bacillus fluorescens,Bacillus fluorescens liquefaciens,Bacterium fluorescens,Liquidomonas fluorescens
D003373	Coumaric Acids	Hydroxycinnamic acid and its derivatives. Act as activators of the indoleacetic acid oxidizing system, thereby producing a decrease in the endogenous level of bound indoleacetic acid in plants.	Coumaric Acid,Hydroxycinnamic Acid,Hydroxycinnamic Acids,Acid, Coumaric,Acid, Hydroxycinnamic,Acids, Coumaric,Acids, Hydroxycinnamic
D004950	Esterases	Any member of the class of enzymes that catalyze the cleavage of an ester bond and result in the addition of water to the resulting molecules.	Esterase
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D014995	Xylosidases	A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds.	Xylobiases,Xylan Hydrolases,Hydrolases, Xylan