In vitro gastrointestinal digestion of pea protein isolate as a function of pH, food matrices, autoclaving, high-pressure and re-heat treatments

被引:60
|
作者
Laguna, Laura [1 ,2 ]
Picouet, Pierre [3 ,5 ]
Dolors Guardia, M. [3 ]
Renard, Catherine M. G. C. [4 ]
Sarkar, Anwesha [1 ]
机构
[1] Univ Leeds, Sch Food Sci & Nutr, Food Colloids & Proc Grp, Leeds LS2 9JT, W Yorkshire, England
[2] CSIC UAM, Inst Food Sci Res CIAL, C Nicolas Cabrera 9, Madrid 28049, Spain
[3] IRTA TA, Food Proc & Engn, Finca Camps I Armet, Monells 17121, Girona, Spain
[4] Avignon Univ, INRA, Securite & Qualite Prod Origine Vegetale, UMR408, F-84000 Avignon, France
[5] Univ Bretagne Loire, INRA, Ecole Super Agr, GRAPPE USC1422, 55 Rue Rabelais, F-49007 Angers, France
关键词
HPP; Autoclave; Digestibility; Puree; Pea protein; PARTICLE-SIZE; DIGESTIBILITY; POLYPHENOLS; NUTRIENTS; PRODUCTS; STARCH; FRUIT;
D O I
10.1016/j.lwt.2017.06.021
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
This study investigated the influence of pH and processing conditions (autoclave at 93 degrees C/13 min or high pressure processing (HPP) at 600 MPa/5 min without/with follow-up reheating at 80 degrees C/30 min) on the digestibility of pea protein isolate. Both aqueous solutions and real food matrices (apple and carrot purees) containing pea protein was examined at 37 degrees C. In vitro gastrointestinal digestion was followed using sodium dodecyl sulphate polyacrylamide gel electrophoresis, titrimetric techniques and theoretical calculations. Pea protein with HPP followed by re-heating showed the highest rate of proteolysis in gastric conditions. In case of sequential intestinal digestion of the gastric chyme, pea protein at pH 6.2 demonstrated higher degree and rate of digestibility as compared to that at pH 3.6, the latter being close to the isoelectric point of pea protein. However, autoclave treatments overshadowed such pH effects. Processing-induced enhancement in digestibility might be attributed to the unfolding of the globular pea protein subunits. Pea protein in the carrot puree was more digestible than in the apple puree, due to apple procyanidins binding to pea protein. These new findings might have important implications in designing the process parameters and selection of appropriate food matrices for delivering pea protein. (C) 2017 Elsevier Ltd. All rights reserved.
引用
收藏
页码:511 / 519
页数:9
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