Complex plant protein prepared from rice protein and pea protein: Improve the thermal stability of betanin
文献类型: 外文期刊
作者: Hu, Ting 1 ; Chen, Jun 1 ; He, Xuemei 2 ; Tang, Yayuan 2 ; Sun, Jian 2 ; Liu, Chengmei 1 ; Dai, Taotao 1 ;
作者机构: 1.Nanchang Univ, State Key Lab Food Sci & Technol, 235 Nanjing East Rd, Nanchang 330047, Peoples R China
2.Guangxi Acad Agr Sci, Nanning 530007, Peoples R China
关键词: Betanin; Thermal stability; Complex plant protein; Interaction
期刊名称:FOOD RESEARCH INTERNATIONAL ( 影响因子:8.1; 五年影响因子:7.7 )
ISSN: 0963-9969
年卷期: 2023 年 164 卷
页码:
收录情况: SCI
摘要: 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 (RPPP) 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 degrees C 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.
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