Abstract
Amylases are enzymes which catalyse the hydrolysis of polysaccharides composed mainly of α-1: 4-linked glucose units, such as starch and its components (amylose and amylopectin), glycogen and certain degradation products derived from these sources. In contrast to phosphorylases (see p. 232), they do not require the presence of phosphate buffer to bring about this hydrolysis. They have been divided into four main categories. — (a) α-Amylases (dextrinogenic or endoamylases) which bring about a rapid fall in viscosity of the substrate solution as a result of the random hydrolysis of glucosidic linkages, followed in the later stages of reaction by the production of reducing sugars (chiefly maltose). (b) ß-Amylases (saccharogenic or exo-amylases) which catalyse the production of maltose from the substrate at an early stage of the reaction without any great loss in viscosity. These enzymes function by an endwise attack on the substrate from the non-reducing ends, (c) Glue-amylases from various micro-organisms which, like ß-amylases, are exoamylases but differ from the two preceding enzymes in that glucose instead of maltose is the end product of their action, (d) The amylase of Bacillus macerans, which produces cyclic (Schardinger) dextrins from the substrates. This enzyme will not be considered in detail.
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Turvey, J.R. (1966). Polysaccharases. In: Bruns, F.H., et al. Enzyme. Handbuch der Physiologisch- und Pathologisch-Chemischen Analyse, vol 6 / b. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-30541-6_27
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