Pepsin activity as a function of pH and digestion time on caseins and egg white proteins under static in vitro conditions-Reference-Cited by-同舟云学术

Pepsin activity as a function of pH and digestion time on caseins and egg white proteins under static in vitro conditions

Published:2021 Issue:24 Volume:12 Page:12468-12478
ISSN:2042-6496
Container-title:Food & Function
language:en
Short-container-title:Food Funct.

Author:

Salelles Léa¹^ORCID,Floury Juliane¹,Le Feunteun Steven¹^ORCID

Affiliation:

1. STLO, INRAE, Institut Agro, 65 rue de Saint-Brieuc, 35042 Rennes, France

Abstract

Protein hydrolysis by pepsin can be substantial under weakly acidic conditions (pH ≥ 4), in particular, for milk caseins which are sensitive to pepsin in a remarkably broad range of pH.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Medicine,Food Science

Link

http://pubs.rsc.org/en/content/articlepdf/2021/FO/D1FO02453A

Reference52 articles.

1. Acid and rennet gels exhibit strong differences in the kinetics of milk protein digestion and amino acid bioavailability

2. Fast and Slow Proteins: Modulation of the Gastric Behavior of Whey and Casein In Vitro

3. Impact of the Dairy Matrix Structure on Milk Protein Digestion Kinetics: Mechanistic Modelling Based on Mini-pig In Vivo Data

4. Slow and fast dietary proteins differently modulate postprandial protein accretion

5. Simulation of the gastric digestion of proteins of meat bolus using a reaction–diffusion model

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