Modelling of pepsin digestibility of myofibrillar proteins and of variations due to heating

Food Chem. 2015 Apr 1:172:265-71. doi: 10.1016/j.foodchem.2014.08.110. Epub 2014 Sep 6.

Abstract

Digestibility of myofibrillar proteins by pepsin was determined by in vitro trials and mathematical modelling. A primary model was developed to predict in vitro digestion kinetics, and a secondary model based on the mechanisms of protein denaturation was then added to take into account the effect of meat heating. Model predictions agreed with measurements in the pH and pepsin concentration ranges 1.8-3.8 and 6-50 U mg(-1) respectively. The utility of the model is illustrated by a simple example where meat is assumed to be heated homogeneously, and myofibrillar proteins to be directly in contact with pepsin. The combined effects of heating time, temperature, enzyme concentration and pH modified the digestibility value, which also depends on residence time in the stomach.

Keywords: Digestion; Enzyme; Gastric; Heating; Kinetics; Model.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Digestion
  • Gastric Mucosa / metabolism
  • Heating
  • Hydrogen-Ion Concentration
  • Models, Theoretical
  • Muscle Proteins / metabolism*
  • Myofibrils / chemistry*
  • Pepsin A / metabolism*

Substances

  • Muscle Proteins
  • Pepsin A