Glucanases Miscellaneous

The jS-D-glucanases which occur in the fission yeast Schizosaccharomyces pom be have been reported. 

In a study of the production of oi-D-glucans by yeasts and yeast-like organisms, most of a total of 177 strains were found able to utilize (1 4)-0f-D-glucans by means of enzymes acting on the reducing ends of the outer D-glucan chains. 

A j8-D-glucanase highly specific for jS-D-glucans containing a linkage sequence (13) has been isolated from several commercial preparations of Bacillus subtilis a-amylase including one purified by repeated crystallization. The 

The properties of new starch-degrading enzymes have been reviewed, Studies on glycogen-storage diseases, concerned mainly with a-D-glucosidases, have also included discussions on amylo-l,4-glucosidase and amylo-l,6-glucosidase activities.  

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. 

A purified e t/o- -D-glucanase from barley was found to be highly specific for the endogenous /S-D-glucan (either in free or dyed form). The enzyme had no action on - 3)- or -(1 4)-linked D-glucans and was inhibited by 

D-Glucose was released from polysaccharides in grape skin and juice by at least one of the polysaccharide hydrolases present in Pectawamorin PI OX .  

The ent/o- -D-glucanase and 8-D-glucanase activities in preparations used in the brewing industry are highest at 50 and 40 °C, respectively, and, in some instances, the stabilities of the enzymes to heat were increased by the presence of substrates.  

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Miscellaneous.—ewcto-j3-D-2-Acetamido-2-deoxyglucanase H from Streptomyces griseus completely hydrolysed the unit A (D-mannose -> 2-acetamido-2-deoxy-D-glucose) glycopeptides of thyroglobulin, but did not act on a modified unit B (a complex heteropolysaccharide) free from side-chains. This and other evidence indicated that this enzyme and an eni/o-/8-D-2-acetamido-2-deoxy-glucanase D from Diplococcus pneumoniae have different specificities the... 

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