Physical and chemical changes of rapeseed meal proteins during toasting and their effects on in vitro digestibility

作     者：Sergio Salazar-Villanea Erik M.A.M.Bruininx Harry Gruppen Wouter H.Hendriks Patrick Carré Alain Quinsac Antonius F.B.van der Poel 

作者机构：Wageningen Livestock ResearchP.O.Box 3386700 AH WageningenThe Netherlands Animal Nutrition GroupWageningen University&ResearchP.O.Box 3386700 AH WageningenThe Netherlands Agfifirm Innovation CenterRoyal Dutch Agrifirm GroupP.O.Box 200187302 HA ApeldoornThe Netherlands Laboratory of Food ChemistryWageningen University&ResearchP.O.Box 176700 AA WageningenThe Netherlands CREOL/OLEAD11 rue MongeParc Industriel33600 PessacFrance Terres Inovia11 rue MongeParc Industriel33600 PessacFrance 

出 版 物：《Journal of Animal Science and Biotechnology》 (畜牧与生物技术杂志（英文版）)

年 卷 期：2017年第8卷第2期

页      面：417-427页

核心收录：

学科分类：090502[农学-动物营养与饲料科学] 0905[农学-畜牧学] 09[农学] 

基　　金：the financial support from the Wageningen UR“IPOP Customized Nutrition”programme financed by Wageningen UR,the Dutch Ministry of Economic Affairs,WIAS,Agrifirm Innovation Center,ORFFA Additives BV,Ajinomoto Eurolysine s.a.s and Stichting VICTAM BV.SSV acknowledges the support from the Universidad de Costa Rica 

主　　题：Hydrolysis rate In vitro protein digestibility Rapeseed meal Reactive lysine Secondary structure 

摘      要：Background： Toasting during the production of rapeseed meal（RSM） decreases ileal crude protein（CP） and amino acid（AA） digestibility. The mechanisms that determine the decrease in digestibility have not been fully elucidated. A high protein quality, low-denatured, RSM was produced and toasted up to 120 min, with samples taken every 20 min. The aim of this study was to characterize secondary structure and chemical changes of proteins and glucosinolates occurring during toasting of RSM and the effects on its in vitro CP ***： The decrease in protein solubility and the increase of intermolecular β-sheets with increasing toasting time were indications of protein aggregation. The contents of NDF and ADIN increased with increasing toasting *** of arginine, lysine and O-methylisourea reactive lysine（OMIU-RL） linearly decreased with increasing toasting time, with a larger decrease of OMIU-RL than lysine. First-order reactions calculated from the measured parameters show that glucosinolates were degraded faster than lysine, OMIU-RL and arginine and that physical changes to proteins seem to occur before chemical changes during toasting. Despite the drastic physical and chemical changes noticed on the proteins, the coefficient of in vitro CP digestibility ranged from 0.776 to 0.750 and there were no effects on the extent of protein hydrolysis after 120 min. In contrast, the rate of protein hydrolysis linearly decreased with increasing toasting time, which was largely correlated to the decrease in protein solubility, lysine and OMIU-RL observed. Rate of protein hydrolysis was more than 2-fold higher for the untoasted RSM compared to the 120 min toasted ***： Increasing the toasting time for the production of RSM causes physical and chemical changes to the proteins that decrease the rate of protein hydrolysis. The observed decrease in the rate of protein hydrolysis could impact protein digestion and utilization.