Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 553976
Title Protein Oxidation and in Vitro Gastric Digestion of Processed Soy-Based Matrices
Author(s) Duque-Estrada, Patrícia; Berton-Carabin, Claire C.; Nieuwkoop, Matthijs; Dekkers, Birgit L.; Janssen, Anja E.M.; Goot, Atze Jan Van Der
Source Journal of Agricultural and Food Chemistry 64 (2019)34. - ISSN 0021-8561 - p. 9591 - 9600.
DOI https://doi.org/10.1021/acs.jafc.9b02423
Department(s) Food Process Engineering
BacGen
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2019
Keyword(s) gastric digestion - meat analogues - processing - protein oxidation - soy proteins
Abstract

Process conditions that are applied to make structured soy-protein-based food commonly include high temperatures. Those conditions can induce protein oxidation, leading to a decrease in their susceptibility to proteolysis by digestive enzymes. We aimed to investigate the effects of thermomechanical processing on oxidation and in vitro gastric digestion of commercial soy protein ingredients. Samples were sheared at 100 to 140 °C and characterized for acid uptake, carbonyl content, electrophoresis, and surface hydrophobicity. The enzymatic hydrolysis was determined in simulated gastric conditions. Protein ingredients were already oxidized and showed higher surface hydrophobicity and hydrolysis rate compared with those of the processed matrices. However, no clear correlation between the level of carbonyls and the hydrolysis rate was found. Therefore, we conclude that gastric digestion is mostly driven by the matrix structure and composition and the available contact area between the substrate and proteolytic enzymes.

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