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Effects of Toasting Time on Digestive Hydrolysis of Soluble and Insoluble 00‐Rapeseed Meal Proteins
Author(s) -
SalazarVillanea Sergio,
Bruininx Erik M. A. M.,
Gruppen Harry,
Carré Patrick,
Quinsac Alain,
Poel Antonius F. B.
Publication year - 2017
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-017-2960-8
Subject(s) - hydrolysis , chemistry , rapeseed , fraction (chemistry) , hydrolyzed protein , maillard reaction , chromatography , enzymatic hydrolysis , food science , biochemistry
Abstract Thermal damage to proteins can reduce their nutritional value. The effects of toasting time on the kinetics of hydrolysis, the resulting molecular weight distribution of 00‐rapeseed meal (RSM) and the soluble and insoluble protein fractions separated from the RSM were studied. Hydrolysis was performed with pancreatic proteases to represent in vitro protein digestibility. Increasing the toasting time of RSM linearly decreased the rate of protein hydrolysis of RSM and the insoluble protein fractions. The extent of hydrolysis was, on average, 44% higher for the insoluble compared with the soluble protein fraction. In contrast, the rate of protein hydrolysis of the soluble protein fraction was 3–9‐fold higher than that of the insoluble protein fraction. The rate of hydrolysis of the insoluble protein fraction linearly decreased by more than 60% when comparing the untoasted to the 120 min toasted RSM. Increasing the toasting time elicited the formation of Maillard reaction products (furosine, N ε ‐carboxymethyl‐lysine and N ε ‐carboxyethyl‐lysine) and disulfide bonds in the insoluble protein fraction, which is proposed to explain the reduction in the hydrolysis rate of this fraction. Overall, longer toasting times increased the size of the peptides resulting after hydrolysis of the RSM and the insoluble protein fraction. The hydrolysis kinetics of the soluble and insoluble protein fractions and the proportion of soluble:insoluble proteins in the RSM explain the reduction in the rate of protein hydrolysis observed in the RSM with increasing toasting time.