Snail 0-glucosidase

Baker s yeast a-D-glucosidase Almond p-D-glucosIdase °Snail p-D-mannosidase... 

Comparison of the Specificites of /3-Glucosidase of Snail and Almond Emulsin... 

The digestive juices of the snail (Helix pomcUia) contain a /S-glucosidase in addition to an active cellulase. In Table XII, the action of the snail emulsin on several jS-glucosides is compared with that of sweet-almond emulsin (43), The snail jS-glucosidase reacts similarly to that in almond emulsin, but the influence of variations in the aglycon structure is much less. 

The specificity of conduritol B epoxide is such that -glucosidases from widely differing sources have been found to react with loss of enzymic activity from various Aspergillus species, > yeast, snail Helix pomatia) sweet almonds, and mammals. The only exceptions have been the / -glucosidases from garbanzo plants Cicer arietum L.) and from Alocasia macrorrhiza The only other enzymes that have been found to be covalently inhibited are a-glucosidase from yeast Saccharo-myces cerevisiae) and the sucrase-isomaltase complex from rabbit small intestine. ... 

The effects of temperature, heat, pH, and trypsin on the -D-glucosidase activity in the digestive juices of the giant snail Achatina balteata have been examined. ... 

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 library of piperidine-based SPH trimers incorporating monomer 42 (Scheme 6) was tested for glycosidase activity. No inhibition was observed for yeast a-glucosi-dase and isomaltase, almond P-glucosidase, human placenta a-fucosidase, snail P-mannosidase, and E. coli P-galactosidase, possibly because of the small number of hydroxyl groups present. 

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