黑曲霉葡糖淀粉酶1颗粒淀粉结合结构域的生产与纯化

Production and purification of a granular-starch-binding domain of glucoamylase 1 from Aspergillus niger.

作者信息

Belshaw N J, Williamson G

机构信息

AFRC Institute of Food Research, Norwich, Norfolk, UK.

出版信息

FEBS Lett. 1990 Sep 3;269(2):350-3. doi: 10.1016/0014-5793(90)81191-p.

DOI:10.1016/0014-5793(90)81191-p

PMID:2119316

Abstract

A domain of glucoamylase 1 from Aspergillus niger which binds to granular starch was produced by proteolytic digestion and purified to apparent homogeneity by extraction with corn starch followed by anion-exchange chromatography and gel filtration. The peptide has a molecular weight of 25,100, contains approximately 38% carbohydrate (w/w) and corresponds to residues 471-616 at the C-terminus of glucoamylase 1. The peptide bound to granular corn starch maximally at 1.08 nmol/mg starch. It inhibited the hydrolysis of granular starch by glucoamylase 1 but had no effect on the hydrolysis of starch in solution.

摘要

黑曲霉葡糖淀粉酶1中与颗粒淀粉结合的结构域通过蛋白水解消化产生，经玉米淀粉提取、阴离子交换色谱和凝胶过滤纯化至表观均一。该肽分子量为25,100，约含38%（w/w）碳水化合物，对应葡糖淀粉酶1 C端的471 - 616位残基。该肽与颗粒玉米淀粉的最大结合量为1.08 nmol/mg淀粉。它抑制葡糖淀粉酶1对颗粒淀粉的水解，但对溶液中淀粉的水解无影响。