Starch, /3-amylase action potato, amylose from

Products.—Considerable information concerning the mechanism of the enzymic hydrolysis of starch has been obtained from investigations of the action of purified maltase-free pancreatic amylase on a number of different substrates. The substrates studied were ordinary unfractionated but exhaustively defatted10 potato and com starches a branched chain substrate, waxy maize starch and amylose, the linear component of corn starch.41 69 eo f4 These investigations included comparisons not only of the rates of the hydrolysis of the different substrates but also of the products formed from them. 

The /3-amylases in the absence of the a-amylases are incapable of degrading whole starches completely. The hydrolysis proceeds rapidly until about 50 to 55 % of the theoretical amount of maltose is produced and then very slowly until a limit of about 61 to 68% is reached (101), The solution is still viscous and the residue, called a /3-amylase limit dextrin, is unfer-mentable. The limit dextrin arises from the inability of /3-amylase to act beyond a branch point in the randomly branched amylopectin molecule and may be envisaged as a pruned amylopectin structure. In the case of potato starch, the /3-limit dextrin includes all the associated phosphate. The limit dextrin contains one end group for every 10 to 12 D-glucose residues (102), in contrast to one in every 25 or 30 residues for the original amylopectin. The initial attack of /3-amylase on amylopectin is about 20 times as fast as on amylose (103), Maltose in amounts of 53 to 62 % of the theoretical have been reported from the action of /3-amylases on amylopec-tins separated from various starches (104). When the /3-limit dextrin is cleaved by acid hydrolysis or by the action of a-amylase, the structure is opened and new chain ends are made available which can be further acted upon by i3-amylase. 

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