Analysis of enzymatic hydrolysis process for preparing active peptides based on protein structure(Ⅰ)Novel 3-D dynamic characterization of enzymatic hydrolysis reaction

QI Wei; HE Zhimin; HE Mingxia

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Analysis of enzymatic hydrolysis process for preparing active peptides based on protein structure(Ⅰ)Novel 3-D dynamic characterization of enzymatic hydrolysis reaction

更新时间：2025-12-10

- Analysis of enzymatic hydrolysis process for preparing active peptides based on protein structure(Ⅰ)Novel 3-D dynamic characterization of enzymatic hydrolysis reaction
- CIESC Journal Issue 12, Pages: 2387-2391(2005)
- 作者机构：
  
  天津大学化工学院化学工程研究所,天津,300072
- 作者简介：
- 基金信息：
- DOI：
  CLC：
- Online First：25 December 2005，
  
  Published：25 December 2005
- 稿件说明：
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QI Wei, HE Zhimin, HE Mingxia. Analysis of enzymatic hydrolysis process for preparing active peptides based on protein structure(Ⅰ)Novel 3-D dynamic characterization of enzymatic hydrolysis reaction[J]. CIESC Journal, 2005, (12): 2387-2391.
DOI：

QI Wei, HE Zhimin, HE Mingxia. Analysis of enzymatic hydrolysis process for preparing active peptides based on protein structure(Ⅰ)Novel 3-D dynamic characterization of enzymatic hydrolysis reaction[J]. CIESC Journal, 2005, (12): 2387-2391. DOI：

摘要

提出了一种基于生物信息学知识与凝胶排阻色谱技术及图形拟合处理相结合的生物大分子复杂酶解反应行为定量分析、直观表征及模拟解析的新方法.研究中以全酪蛋白-胰蛋白酶为模式水解体系，根据完整的HPSEC实验谱图，经分子模拟多肽结构，获得了大量产物多肽信息;绘制了表征酶解反应动态特性的3-D曲面图与21/2维伪彩色图，并对拟合曲面方程进行了数学分析，为调控酶解反应、定向和定量地高效获取目标活性多肽提供了理论依据.

Abstract

A new method was used to analyze

characterize and simulate the kinetic behavior of bio-macromolecular enzymatic hydrolysis reaction based on bio-informatics

HPSEC and graphic processing. Tryptic hydrolysis of whole casein was selected as a model system. The possible reaction mechanism was deduced from a series of chromatographic results and experimental analysis. According to programming calculation and molecular simulation

product information

such as cleavage sites of protein and structure model of active peptides

was also obtained. Furthermore

a 3-D continuous surface and corresponding contour were plotted to characterize the dynamic process of protein enzymatic hydrolysis

and mathematical analysis of the surface-fit function was also carried out. The optimized polynominal equation can be applied to adjustment and control of the complex reaction. It is also beneficial to directional and quantitative preparation of target active peptides.

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