APPLICATION OF ZINC HYDROXIDE IN THE PURIFICATION OF BEAN ALPHA-AMYLASE INHIBITOR

被引：5

作者：

Szamos, J. ^{[1
]}

Maczo, A. ^{[1
]}

Gelencser, E. ^{[1
]}

机构：

[1] Cent Food Res Inst, Dept Biol, H-1022 Budapest, Hungary

来源：

ACTA ALIMENTARIA | 2012年 / 41卷 / 02期

关键词：

bean alpha-amylase inhibitor; zinc hydroxide; protein purification; PHASEOLUS-VULGARIS; SEEDS;

D O I：

10.1556/AAlim.41.2012.2.14

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

A novel step in bean (Phaseolus vulgaris) alpha-amylase inhibitor (AAI) purification, based on the application of an inorganic adsorbent, zinc hydroxide, was developed. The new method was substantially faster than existing protocols. Up to 98% of bean seed proteins were bound to the white precipitate in the range of 1-4% (w/v) zinc hydroxide, while the amount of bound bean AAI was far less in the range of 1-2%. The AAI-enriched fraction, unbound by zinc hydroxide, was further purified by DEAE-(diethylaminoethyl)chromatography and gel filtration. It was found that zinc hydroxide binds the majority of soluble proteins of bean, while it leaves alpha-amylase inhibitor in solution. The binding of proteins to zinc-hydroxide occurs in a short time and the change caused in the buffer composition is insignificant, thus it may open new approaches in purification of other proteins, too.

引用

页码：272 / 276

页数：5

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