Creative Enzymes is proud to be one of the few companies worldwide specifically focused on developing and providing enzyme activity assays. We work closely with customers through the whole process of solving specific problems, optimizing protocols, and developing new assay methods, which helps us well understand the customer’s needs and concerns. Many customers have been loyal to us for years. Creative Enzymes is fully qualified for providing the accurate enzyme activity assays for xylan 1,4-beta-xylosidase.
Xylan 1,4-beta-xylosidase (EC 22.214.171.124; 4-beta-D-xylan xylohydrolase) is an enzyme that hydrolyzes xylooligosaccharides, such as xylobiose and xylotriose, to xylose by recognizing the xylosyl residue at the non-reducing terminal and cleaving the β-1,4 glycosidic linkage. It is a useful enzyme for producing xylose from the xylan of hemicellulose, one of the most abundant biomass resources. Xylan 1,4-beta-xylosidases are currently classified into five families: 3, 39, 43, 52, and 54 of glycoside hydrolases (GH). The catalytic action of xylan 1,4-beta-xylosidase is generally accepted to be a double-displacement mechanism involving a glycosyl-enzyme intermediate, similar to the mechanism of glycosidases. Two essential amino acids play pivotal roles in the enzymatic action of xylan 1,4-beta-xylosidase. The first serves as a nucleophile, attacking the substrate’s anomeric center to form the covalent glycosyl-enzyme intermediate. The second can be used as a general acid/base catalyst, deprotonating the water molecule and attacking the anomeric center to cleave the covalent binding and yield the xylose. Many fungal xylan 1,4-beta-xylosidases have partial similarity to GH3 with the amino acid sequence corresponding to the active site being highly conserved.
Xylan 1,4-beta-xylosidase has gained more and more attention in the biotechnological context. In fact, the use of xylan 1,4-beta-xylosidase in the fermentation of xylose or xylose-containing hydrolysates for ethanol production or bioconversion into xylitol is constantly increasing. Thus, it is essential to monitor the activity of xylan 1,4-beta-xylosidase. Creative Enzymes makes the precise activity measurement available for xylan 1,4-beta-xylosidase. The enzyme activity is assayed using 4-nitrophenyl-β-D-xylopyranoside as substrate. The reaction rate is monitored at 405 nm, indicating the amount of 4-nitrophenol released. Our test results are the most precise and trusted, due to years of testing and discovering various hydrolases. Overall, Creative Enzymes is your trustworthy partner which offers the leading technical support and personalized customer service found nowhere else in the industry.
Figure: The crystal structure of xylan 1,4-beta-xylosidase from Thermoanaerobacterium saccharolyticum.