鹰嘴豆2S白蛋白的纯化及部分特性分析

Purification and partial characterization of chickpea 2S albumin.

作者信息

Vioque J, Sánchez-Vioque R, Clemente A, Pedroche J, Bautista J, Millán F

机构信息

Instituto de la Grasa, Avenida Padre García Tejero 4, Sevilla, Spain.

出版信息

J Agric Food Chem. 1999 Apr;47(4):1405-9. doi: 10.1021/jf980819k.

DOI:10.1021/jf980819k

PMID:10563989

Abstract

A chickpea 2S albumin has been purified by solubilization in 60% methanol and ion-exchange chromatography. Under denaturing conditions it is composed of two peptides of 10 and 12 kDa. Native molecular mass determined by gel filtration chromatography is 20 kDa. Amino acid composition shows that it is rich in sulfur amino acids, mainly cysteine with 4.6% of the total. On the other hand, it has antinutritional characteristics of being allergenic for chickpea-sensitive individuals and inhibitory against porcine chymotrypsin with a lesser degree toward trypsin. The results of interest from a nutritional point of view are discussed.

摘要

一种鹰嘴豆2S清蛋白已通过在60%甲醇中溶解及离子交换色谱法进行了纯化。在变性条件下，它由两条分别为10 kDa和12 kDa的肽组成。通过凝胶过滤色谱法测定的天然分子量为20 kDa。氨基酸组成表明它富含含硫氨基酸，主要是半胱氨酸，占总量的4.6%。另一方面，它具有抗营养特性，对鹰嘴豆敏感个体具有致敏性，对猪胰凝乳蛋白酶有抑制作用，对胰蛋白酶的抑制作用较弱。从营养角度讨论了相关研究结果。