Polysaccharide Hydrolase

About: Polysaccharide Hydrolase is a(n) research topic. Over the lifetime, 28 publication(s) have been published within this topic receiving 415 citation(s).

A novel polysaccharide hydrolase cDNA (celD) from Neocallimastix patriciarum encoding three multi-functional catalytic domains with high endoglucanase, cellobiohydrolase and xylanase activities

Abstract: A plant polysaccharide hydrolase cDNA, designated celD, was isolated from a cDNA library of the rumen fungus Neocallimastix patriciarum. The enzyme encoded by celD had endoglucanase, cellobiohydrolase and xylanase activities. Deletion analysis revealed that celD cDNA can be truncated to code for three catalytically active domains. Each domain had the same substrate specificity as the enzyme produced by the untruncated celD and also possessed cellulose-binding capacity. Substrate competition studies showed that carboxymethylcellulose and xylan appear to compete with methylumbelliferyl cellobioside for the same active site within each domain. Expression of celD transcript in the rumen fungus was constitutive and was not affected by the presence of cellulose in the culture medium.

Bacteriophage Polysaccharide Depolymerases and Biomedical Applications

Abstract: Polysaccharide depolymerase, a polysaccharide hydrolase encoded by bacteriophages (or 'phages'), can specifically degrade the macromolecule carbohydrates of the host bacterial envelope. This enzyme assists the bacteriophage in adsorbing, invading, and disintegrating the host bacteria. Polysaccharide depolymerase activity continues even within biofilms. This effectiveness means phages are promising candidates for novel antibiotic scaffolds. A comprehensive compendium of bacteriophage polysaccharide depolymerases has been compiled, together with their potential biomedical applications, such as novel antibiotics, adjuvants for antibiotics, bacterial biofilm disruptants, and diagnostic kits.

Phage-induced fucosidases hydrolysing the exopolysaccharide of Klebsiella arogenes type 54 [A3(S1)].

Abstract: Several strains of bacteriophage have been isolated that induce the formation of a polysaccharide hydrolase after infection of Klebsiella aerogenes type 54 [A3(S1)]. The action of this enzyme on polysaccharide solutions was to decrease their viscosity and increase their reducing value. These effects were associated with the release of two oligosaccharides (O1 and O2) from the polysaccharide. These two substances are not identical with any of the four oligosaccharides isolated from autohydrolysates. The two enzymically isolated fractions have been tentatively identified as tetrasaccharides, and oligosaccharide O2 is probably an acetylated version of oligosaccharide O1. This latter oligosaccharide differs in some way, still unknown, from the tetrasaccharide cellobiosylglucuronosylfucose found in acid hydrolysates of the slime polysaccharide. The enzyme is limited in its activity to the polysaccharide excreted by the A3 strain of K. aerogenes type 54 or by similar strains. It is also active on the polysaccharides altered by acid or alkaline treatment. The enzyme has optimum activity at pH6·5. A study of the products released by enzyme action has shown it to be a fucosidase splitting the fucosylglucose linkages found in the intact polysaccharide.

Hydrolytic enzymes of some periphytic marine bacteria.

Abstract: Several periphytic marine bacterial cultures were examined for their content of hydrolytic enzymes. Quantitative assays were done for extracellular and intracellular proteinase, phosphatase, esterase, β-glucosidase, and four polysaccharide hydrolase activities. While some of the enzymes were released extracellularly by growing cells, the greatest amounts of proteinase, esterase, phosphatase, and β-glucosidase were located in the cells and released by mechanical breakage or by cell autolysis. Substantial amounts of proteinase were found in washed cell envelopes of the bacteria. All of the bacteria showed some enzymatic activity against one or more of the algal and microbial acid polysaccharides tested. Enzymes active against these polyanions were found either extracellularly or in cell extracts, depending on the culture concerned. Partial lysis of cell envelopes from two of the periphytes was produced by extracellular or intracellular enzyme mixtures. The ecological importance of bacterial hydrolases and t...

Process for preparing oligosaccharide and trans-ferulicacid acid

Abstract: The present invention discloses a preparation process of oligosaccharide and trans-ferulaic acid. Wheat bran, rice bran, bagasse, bean skin and other plant leftover with high polysaccharide content as material is reacted by polysaccharide hydrolase and feruaic acid esterase to produce oligosaccharide and trans-ferulaic acid. The present invention has wide material source, high extraction rate andlow production cost. The production process has mild condition; uses no acid, alkali and other chemical matter; and has no change in the natural property of the product and no environmental pollution.