Revisiting the enzymatic kinetics of pepsin using isothermal titration calorimetry

Q. Luo, Dongxin Chen, R.M. Boom, A.E.M. Janssen*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

51 Citations (Scopus)

Abstract

Pepsin is the first protease that food proteins encounter in the digestive tract. However, most of the previous studies on the enzymatic kinetics of pepsin were based on the hydrolysis of small synthetic peptides, due to the limitations in methodology and the complexity of protein substrate. To better understand the role of pepsin in protein digestion, we used isothermal titration calorimetry to study the enzymatic kinetics of pepsin with bovine serum albumin as the substrate. We found that pepsin has a higher catalytic rate at lower pH, while its affinity to substrate is lower. At the same pH, pepsin has lower activity and affinity at higher ionic strengths. We found contrasting kinetic parameters for pepsin-catalyzed hydrolysis of bovine serum albumin and of small synthetic peptides. Time-dependent kinetics also showed that pepsin has lower efficiency towards intermediate peptides during hydrolysis.
Original languageEnglish
Pages (from-to)94-100
JournalFood Chemistry
Volume268
DOIs
Publication statusPublished - Dec 2018

Keywords

  • Bovine serum albumin
  • Enzymatic kinetics
  • Gastric digestion
  • Isothermal titration calorimetry
  • OPA method
  • Pepsin

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