Interactions between Pea Protein Isolate and Carboxymethylcellulose in Neutral and Acid Aqueous Systems.

Ying Yue,Liya Liu,Litao Tong,Chunhong Li,Lili Wang,Bei Fan,Nana Li,Fengzhong Wang,Shujie Pang

doi:10.3390/foods10071560

Abstract

Pea protein isolate (PPI), as an emerging plant protein, has gradually aroused the attention of the public, but the PPI, especially high-concentration PPI’s low stability in the acidic aqueous system, was still a problem that limited its application. In this research, we investigated the interactions between relatively high concentrations of PPI (3.0%) and carboxymethylcellulose (CMC, 0–0.5%) in neutral and acid aqueous systems to explore the change of the phase behavior and stability of PPI as affected by CMC. It showed that the stability of PPI in the aqueous systems strongly depended on the CMC concentration, especially at the acidic aqueous systems. At neutral aqueous system, a certain amount addition of CMC into the PPI caused serious phase separation. While stable PPI solutions can be obtained at a narrow region around pH 4.5 to 5.5 by adding different amounts of CMC. The enhancement in the electrostatic repulsion and steric hindrance between the newly formed PPI-CMC biopolymers, as well as the increase in bulk viscosity with the adding of CMC at pH 4.5, contributed to the higher stability of PPI in acidic aqueous systems.

Highlights

Proteins, as their solubility, emulsifying capabilities, foaming and rheological behaviors, and some other functional properties, have been widely used in the food industry [1].In recent years, there is a preferred alternative to replace animal-based protein sources with plant proteins due to the latter’s lower costs, sustainability, and lower carbon footprint and their benefits in cardiovascular health and physiological effects [2,3].The pea, as the second most important leguminous crop, is rich in proteins [4]
It can be seen that the individual Pea protein isolate (PPI) sample formed precipitate at pH ≤ 5.5, which might due to the protein syneresis and denaturation cause the aggregation of PPI
The mixed peapea protein isolatecarboxymethylcellulose (PPI-CMC) solutions remained quite stable at a pH of 5 might be the complexation of PPI and CMC provide more negative charges on the su of thebeprotein which inhibited aggregation ofnegative the PPIcharges at theon acidic environmen might the complexation of PPI andthe provide more the surface

Summary

Introduction

As their solubility, emulsifying capabilities, foaming and rheological behaviors, and some other functional properties, have been widely used in the food industry [1].In recent years, there is a preferred alternative to replace animal-based protein sources with plant proteins due to the latter’s lower costs, sustainability, and lower carbon footprint and their benefits in cardiovascular health and physiological effects [2,3].The pea, as the second most important leguminous crop, is rich in proteins (around20–25%) [4]. There is a preferred alternative to replace animal-based protein sources with plant proteins due to the latter’s lower costs, sustainability, and lower carbon footprint and their benefits in cardiovascular health and physiological effects [2,3]. The pea protein has been utilized as emerging plant protein ingredients in plant-based foods to replace animal-based protein due to its high nutritional value, nonGM, sustainable, and functional benefits [5]. Plant-based beverages are often prepared with whole or peeled seeds, and protein extracts [6]. The use of pea protein isolate (PPI) in the fields of preparing protein-fortified beverages and pea milk is quite popular in recent years. Different from other legume proteins (such as faba bean, lentil, and chickpea), PPI was reported to exhibit very low stability in the acidic aqueous system due to its poor functional characteristics [7,8,9], which limits its application in acidic protein beverages and yogurt products

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Conclusion