Kinetics of the surface hydrolysis of raw starch by glucoamylase.
Kinetics of the surface hydrolysis of raw starch by glucoamylase.
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DOI：
10.1021/jf050934c
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发表时间：
2005-09
影响因子：
6.1
通讯作者：
Hirosuke Tatsumi;H. Katano
中科院分区：
文献类型：
--
作者：
Hirosuke Tatsumi;H. Katano
用安培型葡萄糖传感器研究了不同粒径的淀粉颗粒在糖化酶催化下的水解反应。在原淀粉悬浮液中的酶解的初始速率随着酶浓度的增加而增加，接近饱和值，并且与底物的量成正比。此外，速率与基底的比表面积成比例。实验结果可以很好地解释了从一个三步机制，其中包括自由酶的吸附到基板的表面上，吸附的酶与基板的反应，并释放的产物的速率方程。
The hydrolysis of raw starch catalyzed by glucoamylase has been studied with starch granules of different sizes by use of an amperometric glucose sensor by which the direct and continuous observation of the concentration of glucose can be achieved even in a thick raw starch suspension. The initial rate of the enzymatic hydrolysis in the raw starch suspension increased with increasing concentration of the enzyme to approach a saturation value and was proportional to the amount of substrate. Also, the rate was proportional to the specific surface area of the substrate. The experimental results can be explained well by the rate equations derived from a three-step mechanism, which consists of adsorption of the free enzyme onto the surface of the substrate, reaction of the adsorbed enzyme with the substrate, and liberation of the product.