P-l,3-D-Glucanases

An Acinetobacter sp. growing on cells of baker s yeast as the only source of carbon secreted an e do-P-l,3-D-glucanase activity.  

The synthesis of polysaccharide hydrolases, including endo-p-l,4-D-glucanases, by germinating rye has been examined.  

Among other activities, glucanase GV (a commercial enzyme preparation of fungal origin) contains an cndo-P-l,4-D-glucanase, which could be separated from an endogenous cxo-P-l,3-D-glucanase by gel filtration.  

Among other activities, glucanase GV contains an exo-P-l,3-D-glucanase which has a relatively high specificity for (1 - 3)-P-D-glucosidic linkages, but which does not attack lichenin.  

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A new, improved assay of emfo-P-l,3-D-glucanases, which combines the simplicity of a reductiometric method with the specificity of a viscosimetric method, measures the amount of blue dye released from a Cibachron Blue derivative of pachyman. ... 

Purification of an endo-p-l,3-D-glucanase from a green-malt extract gave a fraction containing two protein components, one of which is enzymically active. This enzyme (p7 9.8) was stimulated by sodium chloride and exhibited optimal activity towards laminarin and carboxymethylpachyman at pH 5,0 and 5.8,... 

A purified exo-p-l,3-D-glucanase obtained from culture fluids of the yeast Candida utilis contains a high proportion of acidic amino-acids and 20% of carbohydrate, is more reactive towards laminarin than towards 4-nitrophenyl P-D-glucopyranoside and the (1 - 3)-p-D-glucans in yeast cell walls, and is strongly inhibited by lactones and some heavy-metal ions. ... 

The hydrolysis of pachyman [a (1 3)-p-D-glucan] by culture filtrates of more than 700 strains of micro-organisms has been examined. Several commercial and gastropode enzyme preparations were also tested for P-l,3-D-glucanase activity. A strain of Streptomyces, which is related to S. arabicus, synthesizes an appreciable amount of P-l,3-D-glucanase activity. 

Commercially available enzymes used in the preparation of fungal cell walls have been examined for a- and P-D-glucanases, including p-l,3-D-glucanase. ... 

Comparison of the properties of the p-l,3-D-glucanases (laminarinases) from Aspergillus nidulans, a Basidiomycetes sp., and Trichoderma viride showed that the enzyme from A. nidulans differs in its action on laminarin. ... 

Two P-l,3-D-glucanases that degrade yeast cell walls have been isolated from culture media of Bacillus circulans by adsorption onto a yeast D-glucan. One of the enzymes of mol. wt. 4 x 10 hydrolysed laminarin (K 0.105 mol 1 , pH optimum 5.5 cf. the pH optimum of 6.5 for the other enzyme) to laminaribiose and D-glucose, and had a synergistic effect on a lytic P-l,6-D-glucanase from the same bacterium. 

Extracellular e/u/n-j3-l,6-D>glucanase was produced in high concentration when Bacillus circulans was grown on yeast cell walls (see also p. 368). This enzyme was separated from the e/idb-jS-l,3-D-glucanase by gel filtration, and was then purified by ion-exchange chromatography. The enzyme exhibited maximal activity at pH 5.5 but, in contrast to the crude culture fluid, had only a limited action on the cell walls of yeast or Schizosaccharomyces pombe. 

Both exo-P-l,6- and eAro-jS-l,3-D-glucanase activities present in cell extracts and culture fluids of Schizosaccharomyces japonicus appear to be manifest by the same species. ... 

Damascene, C.M.B., Bishop, J.G., RipoU, D.R., Win, J., Kamoun, S., Rose, J.K.C. (2008). Structure of the glucanase inhibitor protein (GIP) family from Ph5dophthora species suggests coevolution with plant endo-P-l,3-glucanases. Mol. Plant-Microbe Interact. 21, 820-830. 

A neutral a-D-glucosidase from porcine serum preferentially hydrolysed malto-oligosaccharides. The substrate specificity and kinetic properties, etc., of a jS-l,4-D-glucanase (mol. wt. 5.1 x 10 pH optimum 5.5—6.0, temperature optimum 45 °C) isolated from the intestinal juices of a snail Helixpomatia) have been determined. The purified enzyme, which degrades poly- and oligosaccharides (d.p. >3) containing /8-(l -> 4)- and j8-(l 3)-linked D-glucosyl residues, was inhibited by Hjedta and appeared to be activated by Ca + ions. 

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