Kinetic model for the co-action of beta-amylase and debranching enzymes in the production of maltose.
The kinetics of the hydrolysis of starch with beta-amylase and debranching enzymes was studied. The hydrolysis of the alpha-1, 6-glycoside bonds of the substrate by debranching enzymes does not create any new nonreducing ends, so debranching enzyme promotes the action of beta-amylase not by increasing the concentration of the substrate of beta-amylase but by increasing the linear linkage portion of the substrate. The introduction of an effective chain length function was used to formulate a kinetic model.
Jiahua
Z
Z
Department of Chemical Engineering, Guangdong University of Technology, Dongfeng Road 729, Guangzhou, People's Republic of China. hgx@gdut.edu.cn
D001709:Biotechnology; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008320:Maltose / Q000096:biosynthesis*; D008954:Models, Biological; D013213:Starch / Q000378:metabolism; D013379:Substrate Specificity; D001614:beta-Amylase / Q000378:metabolism*
D008320:Maltose; D013213:Starch; D006026:Glycoside Hydrolases; D001614:beta-Amylase; C100181:pullulanase