The kinetics of the hydrolysis of soluble starch by simultaneous use of ,&amylase and either isoamylase or pullulanase was studied experimentally for a wide range of substrate and enzyme concentrations. A kinetic expression was constituted for maltose production by P-amylase, which was stimulated by
Kinetic model for the co-action of β-amylase and debranching enzymes in the production of maltose
✍ Scribed by Zhou Jiahua
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 224 KB
- Volume
- 62
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
The kinetics of the hydrolysis of starch with -amylase and debranching enzymes was studied. The hydrolysis of the ␣-1,6-glycoside bonds of the substrate by debranching enzymes does not create any new nonreducing ends, so debranching enzyme promotes the action of -amylase not by increasing the concentration of the substrate of -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.
📜 SIMILAR VOLUMES
Quinones have been considered as reactive compounds present on the surface of active carbon. Thus, the co-catalytic use of quinones combined with the phosphovanadomolybdate polyoxometalate, PV2Mo10O40(5-), has been studied as an analogue of the known PV2Mo10O405-/C catalyst in oxidative dehydrogenat