Purification and characterization of Kunitz trypsin inhibitor from soybean

被引：0
作者：
Gu, Chunmei [1 ]
Li, Shujun [1 ]
Song, Xinxiu [1 ]
机构：
[1] Jilin Agr Univ, Inst Food Sci & Engn, Changchun 130118, Jilin, Peoples R China
来源：
PROCEEDINGS OF THE 2017 6TH INTERNATIONAL CONFERENCE ON ENERGY, ENVIRONMENT AND SUSTAINABLE DEVELOPMENT (ICEESD 2017) | 2017年 / 129卷
基金：
中国国家自然科学基金;
关键词：
soybean; Kunitz trypisin inhibitor; purification; characterization; SEEDS;
D O I：
暂无
中图分类号：
T [工业技术];
学科分类号：
08 ;
摘要：
In this paper, a Kunitz trypsin inhibitor from soybean meal was isolated to apparent homogeneity by a combination of phosphoric acid extraction, heat treatment, ammonium sulfate precipitation, ion exchange chromatography, affinity chromatography and gel filtration. The results showed that the specific activity of 4733 U mg(-1) and purification fold of 72.39 were obtained. The purified Kunitz trypsin inhibitor appeared a single protein band in SDS-PAGE electrophoresis. The accurate molecular mass of this inhibitor was determined as 22907.51Da by MALDI-TOF. Partial amino acid sequence of the purified protein from Edman degration showed a high degree of homology with various members of the Kunitz-inhibitor family.
引用
收藏
页码：659 / 666
页数：8
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