Impact of processing conditions and structural matrix differences on in vitro protein digestibility of potato, pea and rice proteins

Luis Miguel Jimenez Munoz

Research output: Book/anthology/dissertation/reportPh.D. thesis

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Abstract

The raise in the availability of protein ingredients from plant sources during this decade has generated diverse opportunities for their incorporation in more nutritious and sustainable foods. Efforts aimed to characterize the ingredients from a sensory, functional and nutritional perspective, are required to successfully understand their incorporation in food matrices. It is then of utmost importance to apply principles leading to the design of food structures that will ensure optimal function. Current efforts aim to improve the ingredients’ processing functionality and to provide product formulation with appropriate essential amino acids balance. For this reason it is necessary to study the molecular interactions occurring during isolation and processing of the ingredients, as the processing history provides the basis of supramolecular structures present in the food matrix, and their impact on digestibility. The present research focused on the how extraction and processing conditions may affect the structure formation during gastrointestinal digestion, and its consequences on the in vitro protein digestibility. Three plant proteins sources (pea, potato and rice) were studied utilizing the standardized static and semi-dynamic INFOGEST in vitro digestion system. The results demonstrate that processing history, composition and structure of the protein matrices have a significant effect on protein digestibility. It was clearly shown that, in the case of pea and potato protein ingredients still present with native protein structures, pre-heating of the dispersions before digestion improved protein digestibility, most likely by causing increased hydration, protein dissociation and unfolding, which facilitated accessibility to proteases. In the case of potato protein digestion, although heat treatment reduced trypsin inhibitory activity, this could not be considered the determining factor to the increased digestibility. The use of different protein matrices with the same protein composition also showed that the structure had an impact in gastric emptying; for instance, heat-set foams are more resistant to breakdown and gastric emptying than dispersions or unheated foams. In this work, in vitro DIAAS was also calculated from for potato proteins, and showed that the DIAAS was higher for heated thank unheated matrices. This research contributed to an improved utilization of specific plant protein ingredients in food matrices with high potential for human consumption.
Original languageEnglish
Number of pages176
Publication statusPublished - Oct 2022

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