Complex plant protein prepared from rice protein and pea protein: Improve the thermal stability of betanin. (February 2023)

• Record Type: Journal Article
• Authors: Hu, Ting; Chen, Jun; He, Xuemei; Tang, Yayuan; Sun, Jian; Liu, Chengmei; Dai, Taotao
• Is Part Of: Food research international. Volume 164(2023)
• Publication Date: 2023-02
• Subjects: Betanin -- Thermal stability -- Complex plant protein -- Interaction; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2022.112341
• Languages: English
• ISSNs: 0963-9969

Abstract

Graphical abstract: Highlights: Rice-pea complex plant protein highly improved the thermal stability of betanin. The main interaction between RP-PP and betanin was hydrophobic interaction. RP-PP had a porous network structure and aggregated after binding with betanin. The protective effect of RP-PP on betanin was due to its interaction and encapsulation. Abstract: Betanin (BN) is a kind of edible natural red pigment with a variety of biological activities, but the thermal instability of BN has critically restricted its application in food industry. In this study, complex plant protein (RP-PP) was constructed by rice protein (RP) and pea protein (PP) to study the thermal protection effect and protective mechanism on BN. Thermal degradation results indicated RP-PP significantly improved thermal protection effect, and the degradation rate of BN was decreased from 93.74 % to 56.48 % after heating at 80 ℃ for 60 min. The main interaction between RP-PP and BN was hydrophobic force based on the result of fluorescence spectroscopy, FTIR and molecular docking. In addition, a porous network structure of RP-PP was observed by SEM, and the pore structure gradually decreased at the presence of BN, which speculated BN was trapped in it. TEM observation showed that RP-PP gradually aggregated with the increasing BN concentration, leading to a significant increase in particle size and the formation of network structure. The BN acted as a bridge to the surrounding proteins in the aggregated complex and was encapsulated within it. The interaction and encapsulation may be the key reasons for the improved thermal stability of BN.