Abstract
The hydrolysis of waxy-maize amylopectin and its beta-amylolysis limit dextrin by the alpha-amylase of Bacillus subtilis was followed by gel filtration on Sepharose CL-6B. The mixture of alpha-dextrins was also treated with beta-amylase. The d.p. of these β-limit dextrins was similar to those of the products obtained when the amylopectin β-limit dextrin was the substrate. It is suggested that amylopectin and its β-limit dextrin are hydrolysed by the alpha-amylase by fission of longer internal chains between unit clusters. A model is presented which shows how these unit clusters can be connected to build up the amylopectin molecule. Maltohexaose was produced from the amylopectin, but not from the amylopectin β-limit dextrin, and it is concluded that the latter is produced solely from the external chains.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
