|Table of Contents|

Purification, Characterization of a Trypsin Inhibitor from Black Soybean ［Glycine max(L.) merr.］ and Effect of High Temperature on Its Digestion(PDF)

《大豆科学》[ISSN:1000-9841/CN:23-1227/S]

Issue:
2019年04期
Page:
597-606
Research Field:
Publishing date:

Info

Title:
Purification, Characterization of a Trypsin Inhibitor from Black Soybean ［Glycine max(L.) merr.］ and Effect of High Temperature on Its Digestion
Author(s):
SU Zi-jian1;  SUN Le-chang1; 2;  YAN Long-jie1;  ZHANG Ling-jing1; 2;  LIU Guang-ming1; 2;  CAO Min-jie1; 2
(1.College of Food and Biological Engineering,Jimei University,Xiamen 361021, China; 2.National & Local Joint Engineering Research Center of Processing Technology for Aquatic Products, Xiamen 361021, China)
Keywords:
Purification;  Black soybean;  Trypsin inhibitor;  Inhibition;  Digestion
PACS:
-
DOI:
10.11861/j.issn.1000-9841.2019.04.0597
Abstract:
Trypsin inhibitor (TI) has significant research value in food science and biotechnology. In order to investigate the properties of black soybean trypsin inhibitor (BSTI) and the digestive properties of gastrointestinal fluids, BSTI was purified from black soybeans by degreasing, heat treatment, ammonium sulfate salting out and anion column chromatography. SDS-PAGE showed a single band of BSTI with a relative molecular mass of approximately 21 kDa. BSTI was stable below 60℃ and in the range of pH2-11. When the molar ratio of BSTI to trypsin reached 1, the activity of trypsin was suppressed to 15% or less. Inhibition kinetics indicated that the inhibition of trypsin by BSTI was non-competitive type, and its inhibition constantKi=0.24 nmol?L-1. The results of circular dichroism analysis showed that the secondary structure of BSTI at room temperature wasβ-sheet 43.4%, random coil 29.0%,β-turn 21.2%,α-helix 8.1% and its denaturation temperature was 61±0.9℃. BSTI was resistant to simulated gastrointestinal fluid digestion. However, after heat treatment at 121℃ for 30 min, the anti-enzymatic action of BSTI was significantly reduced, and was easily hydrolyzed by major digestive enzymes such as pepsin, trypsin and chymotrypsin.

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Last Update: 2019-07-25