α-アミラーゼの米タンパク質への吸着 : 清酒もろみにおける蒸し米の溶解機構(第6報)

概要

論文の詳細を見る
Proteins were separated from white rice and adsorption of α-amylase onto the proteins was examined. α-Amylase was adsorbed well onto the oryzenin fraction but not onto the prolamin fraction ; the globulin fraction was intermediate (adsorption efficiency : 78%). The maximum adsorption of α-amylase was 800-1,000 units/mg oryzenin fraction. The optimum pH for the adsorption was 4. The adsorption efficiency differed depending on the organic acids used for the buffer solution ; α-amylase was adsorbed completely in lactate and acetate buffers (25 mM, pH 4.5) but only less than 20% in tartarate, oxalate and citrate buffers (25 mM, pH 4.5). The adsorption efficiency decreased with higher concentrations of buffer solution and salt solution ; α-amylase was not adsorbed at 100 mM lactate buffer, 10 mM citrate buffer or 50 mM NaCl solution. Adsorption of α-amylase onto the oryzenin fraction decreased on treating the protein with DNFB (2,4-Dinitro-fluorobenzene) or DNS (Dansyl chloride). These results coincided with the adsorption of α-amylase onto steamed rice or rice powder.
社団法人日本生物工学会の論文
1982-05-25