Abstract Enzymatic hydrolyses of proteins are established processes to release functional peptides that can be used in various food applications. Prediction of hydrolysate composition requires detailed knowledge and understanding of the reaction dynamics of protein breakdown and peptide release. Therefore, degradation of the model substrate β-lactoglobulin, and the time-dependent release and hydrolysis of, in total, 59 peptides were characterised during tryptic hydrolysis (37 °C, pH 8.0, E/S-ratio 0.1%). These data were used to parametrise a parsimonious, generally applicable mathematical model that describes the formation of an enzyme-substrate-complex as a second-order reaction and the release of products via degradation of the complex as first-order reaction. To improve the fit of the model, a dependency of the reaction rate constant on the peptide length of the hydrolysis substrate was included. As only general characteristics are used, the proposed model is easy to use and can give a rough prediction of hydrolysate composition.

中文翻译：

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β-乳球蛋白的胰蛋白酶水解：描述肽水解动力学和释放的通用方法

摘要 蛋白质的酶促水解是释放可用于各种食品应用的功能性肽的成熟过程。水解产物组成的预测需要详细的知识和对蛋白质分解和肽释放的反应动力学的理解。因此，模型底物 β-乳球蛋白的降解以及总共 59 种肽的时间依赖性释放和水解在胰蛋白酶水解（37°C，pH 8.0，E/S 比 0.1%）期间被表征。这些数据用于参数化一个简单的、普遍适用的数学模型，该模型将酶-底物-复合物的形成描述为二级反应，并将通过复合物降解的产物释放描述为一级反应。为了提高模型的拟合度，包括反应速率常数对水解底物肽长度的依赖性。由于仅使用一般特征，所提出的模型易于使用，并且可以粗略地预测水解物的组成。