α-アミラーゼのα米粉末への吸着

概要

論文の詳細を見る
α-Rice (steamed and dehydrated with alcohol) was pulverized in a Vibrating Mill and particles smaller than 100 mesh were collected. Adsorption of α-amylase onto the α-Rice powder was found to follow a curve similar to Langmuir's isotherm; but the adsorption decreased little as the volume of enzyme solution increased, with the same total amount of α-amylase, i.e., with decreasing concentration of the enzyme solution.α-Rice was pulverized into particles of various sizes. They were divided into 5 fractions : 30-60 mesh (I), 60-100 mesh (II), 100-150 mesh (III), 150-200 mesh (IV), and more than 200 mesh (V).These fractions were further pluverized to fine particles of smaller than 200 mech and adsorption of α-amylase on to these particles was investigated. Repulverized fraction I adsorbed about 6,000 units of α-amylase/g-powder, as opposed to about 3,500 units/g-powder by fraction V. This suggests that internal structure of α-rice grain heterogeneous, resulting in fine and coarse particles on pulverization, and the coarser particles adsorb more α-amylase.α-Amylase adsorbed onto α-rice could react with soluble starch, though its activity was lower than that of the free enzyme.
社団法人日本生物工学会の論文