Zhuojia Lin , Jialing Chen , Zixi Liu , Xiang Li , Zhili Wan , Xiaoquan Yang
{"title":"自凝聚法制备豌豆蛋白:理化性质及乳化性质","authors":"Zhuojia Lin , Jialing Chen , Zixi Liu , Xiang Li , Zhili Wan , Xiaoquan Yang","doi":"10.1016/j.foodhyd.2025.111995","DOIUrl":null,"url":null,"abstract":"<div><div>Self-coacervation is a promising method of mild protein extraction to obtain high-purity plant proteins that retain the native protein structure and have satisfactory functionality. This study prepared the novel pea protein isolates by the self-coacervation process in dispersions of pea flour (F-PPI) and pea protein-concentrated flour via air classification (C-PPI), and then investigated their discrepancies with the conventional pea protein isolate (PPI) extracted by the alkali solubilization and acid precipitation at different pH conditions. The results showed that at neutral conditions (pH 7.0), the solubility, structural stability, interfacial activity, and emulsifying properties of F-PPI and C-PPI solutions possessed comparable performances with PPI. However, at pH 3.5, the former displayed significantly improved structural and functional properties. This is attributed to the fact that the F-PPI and C-PPI had a higher isoelectric point of around pH 5.3 than PPI (pH 4.8), thus endowing these proteins with lower protein aggregation and better functional activity under acidic conditions. Oral tribological measurements revealed that compared to the PPI-based emulsions, the emulsions stabilized by F-PPI and C-PPI had superior oral lubrication capacity at both pH 7.0 and 3.5. However, after the addition of saliva, the friction coefficient of F-PPI and C-PPI stabilized emulsions increased, leading to a reduced lubricating effect. This can be explained by their interactions with salivary mucin, leading to the flocculation of oil droplets (pH 7.0) and an increase in emulsion viscosity (pH 3.5). These findings demonstrate that the self-coacervation can be used as an efficient, mild protein extraction method for preparing the naturally low-denatured pea proteins, especially under acidic conditions.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111995"},"PeriodicalIF":11.0000,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Pea proteins prepared by self-coacervation: Physicochemical characterization and emulsifying properties\",\"authors\":\"Zhuojia Lin , Jialing Chen , Zixi Liu , Xiang Li , Zhili Wan , Xiaoquan Yang\",\"doi\":\"10.1016/j.foodhyd.2025.111995\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Self-coacervation is a promising method of mild protein extraction to obtain high-purity plant proteins that retain the native protein structure and have satisfactory functionality. This study prepared the novel pea protein isolates by the self-coacervation process in dispersions of pea flour (F-PPI) and pea protein-concentrated flour via air classification (C-PPI), and then investigated their discrepancies with the conventional pea protein isolate (PPI) extracted by the alkali solubilization and acid precipitation at different pH conditions. The results showed that at neutral conditions (pH 7.0), the solubility, structural stability, interfacial activity, and emulsifying properties of F-PPI and C-PPI solutions possessed comparable performances with PPI. However, at pH 3.5, the former displayed significantly improved structural and functional properties. This is attributed to the fact that the F-PPI and C-PPI had a higher isoelectric point of around pH 5.3 than PPI (pH 4.8), thus endowing these proteins with lower protein aggregation and better functional activity under acidic conditions. Oral tribological measurements revealed that compared to the PPI-based emulsions, the emulsions stabilized by F-PPI and C-PPI had superior oral lubrication capacity at both pH 7.0 and 3.5. However, after the addition of saliva, the friction coefficient of F-PPI and C-PPI stabilized emulsions increased, leading to a reduced lubricating effect. This can be explained by their interactions with salivary mucin, leading to the flocculation of oil droplets (pH 7.0) and an increase in emulsion viscosity (pH 3.5). These findings demonstrate that the self-coacervation can be used as an efficient, mild protein extraction method for preparing the naturally low-denatured pea proteins, especially under acidic conditions.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"172 \",\"pages\":\"Article 111995\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-09-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Hydrocolloids\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0268005X25009555\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X25009555","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Pea proteins prepared by self-coacervation: Physicochemical characterization and emulsifying properties
Self-coacervation is a promising method of mild protein extraction to obtain high-purity plant proteins that retain the native protein structure and have satisfactory functionality. This study prepared the novel pea protein isolates by the self-coacervation process in dispersions of pea flour (F-PPI) and pea protein-concentrated flour via air classification (C-PPI), and then investigated their discrepancies with the conventional pea protein isolate (PPI) extracted by the alkali solubilization and acid precipitation at different pH conditions. The results showed that at neutral conditions (pH 7.0), the solubility, structural stability, interfacial activity, and emulsifying properties of F-PPI and C-PPI solutions possessed comparable performances with PPI. However, at pH 3.5, the former displayed significantly improved structural and functional properties. This is attributed to the fact that the F-PPI and C-PPI had a higher isoelectric point of around pH 5.3 than PPI (pH 4.8), thus endowing these proteins with lower protein aggregation and better functional activity under acidic conditions. Oral tribological measurements revealed that compared to the PPI-based emulsions, the emulsions stabilized by F-PPI and C-PPI had superior oral lubrication capacity at both pH 7.0 and 3.5. However, after the addition of saliva, the friction coefficient of F-PPI and C-PPI stabilized emulsions increased, leading to a reduced lubricating effect. This can be explained by their interactions with salivary mucin, leading to the flocculation of oil droplets (pH 7.0) and an increase in emulsion viscosity (pH 3.5). These findings demonstrate that the self-coacervation can be used as an efficient, mild protein extraction method for preparing the naturally low-denatured pea proteins, especially under acidic conditions.
期刊介绍:
Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication.
The main areas of interest are:
-Chemical and physicochemical characterisation
Thermal properties including glass transitions and conformational changes-
Rheological properties including viscosity, viscoelastic properties and gelation behaviour-
The influence on organoleptic properties-
Interfacial properties including stabilisation of dispersions, emulsions and foams-
Film forming properties with application to edible films and active packaging-
Encapsulation and controlled release of active compounds-
The influence on health including their role as dietary fibre-
Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes-
New hydrocolloids and hydrocolloid sources of commercial potential.
The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.