米糠胰蛋白酶抑制剂的纯化与特性分析
Purification and characterization of a trypsin inhibitor from rice bran.
作者信息
Tashiro M, Maki Z
出版信息
J Nutr Sci Vitaminol (Tokyo). 1979;25(3):255-64. doi: 10.3177/jnsv.25.255.
A trypsin inhibitor was isolated and purified from the bran of rice, Oryza sativa, by extraction with 1% sodium chloride, heat treatment, ammonium sulfate precipitation, ion-exchange chromatography on a CM-Sephadex C-25 and gel filtration on a Sephadex G-75. The final preparation was homogeneous by electrophoretic analysis. Rice bran trypsin inhibitor (RBTI) had a molecular weight of about 14,500 and an isoelectric point of 8.07. The amino acids, acid composition was characterized by high contents of basic amino acids, aspartic acid, glutamic acid, proline and cystine. BRTI inhibited bovine trypsin at an inhibitor-enzyme molar ratio of 1:1.6. It displayed, however, nobility to inhibit alpha-chymotrypsin, pepsin, papain and subtilisin BPN'.
通过用1%氯化钠提取、热处理、硫酸铵沉淀、在CM-葡聚糖凝胶C-25上进行离子交换色谱以及在葡聚糖凝胶G-75上进行凝胶过滤，从水稻（Oryza sativa）的麸皮中分离并纯化出一种胰蛋白酶抑制剂。通过电泳分析，最终制剂呈均一状态。米糠胰蛋白酶抑制剂（RBTI）的分子量约为14,500，等电点为8.07。其氨基酸组成的特点是碱性氨基酸、天冬氨酸、谷氨酸、脯氨酸和胱氨酸含量较高。BRTI以1:1.6的抑制剂-酶摩尔比抑制牛胰蛋白酶。然而，它对α-糜蛋白酶、胃蛋白酶、木瓜蛋白酶和枯草杆菌蛋白酶BPN'没有抑制作用。
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