Lijuan Luo , Ping Li , Yuanyuan Deng , Guang Liu , Yan Zhang , Xiaojun Tang , Pengfei Zhou , Zhihao Zhao , Jiarui Zeng , Mingwei Zhang
{"title":"酶法脱酰胺增强豌豆蛋白凝胶的凝胶化和营养特性","authors":"Lijuan Luo , Ping Li , Yuanyuan Deng , Guang Liu , Yan Zhang , Xiaojun Tang , Pengfei Zhou , Zhihao Zhao , Jiarui Zeng , Mingwei Zhang","doi":"10.1016/j.foodhyd.2025.111968","DOIUrl":null,"url":null,"abstract":"<div><div>Pea protein exhibits poor gelation properties due to low cysteine content, limiting its application as a structural ingredient in food systems. This study investigated the effects of enzymatic deamidation on calcium-induced thermal gelation of pea protein and elucidated the mechanism of improved digestibility through microstructural modification. Results show that enzymatic deamidation significantly improves calcium-induced thermal gelation of pea protein isolate, reducing minimum gelation concentration from 9 % to 3 % and increasing calcium tolerance from 20 mM to 40 mM compared to native pea protein isolate (NPPI). Microstructural analysis revealed deamidated PPI (DPPI) formed homogeneous fine-stranded networks, while NPPI developed rough porous networks composed of large-sized protein aggregates. This structural transformation, attributed to increased carboxyl groups facilitating calcium bridging, enhanced gel strength, water-holding capacity, and digestive nutritional properties. The fine-stranded network structure of DPPI gels significantly improved protein digestibility (68–86 % vs. 57 %) and calcium bioavailability (85–90 % vs. 77 %) by promoting contact between digestive enzymes and protein substrates, increasing the accessibility of cleavage sites and facilitating the release of calcium-peptide complexes. Deamidation offers a promising strategy for creating pea protein gels with superior functionality and nutritional value.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111968"},"PeriodicalIF":11.0000,"publicationDate":"2025-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Enhancement of protein gelation and nutritional properties in pea protein gels through enzymatic deamidation\",\"authors\":\"Lijuan Luo , Ping Li , Yuanyuan Deng , Guang Liu , Yan Zhang , Xiaojun Tang , Pengfei Zhou , Zhihao Zhao , Jiarui Zeng , Mingwei Zhang\",\"doi\":\"10.1016/j.foodhyd.2025.111968\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Pea protein exhibits poor gelation properties due to low cysteine content, limiting its application as a structural ingredient in food systems. This study investigated the effects of enzymatic deamidation on calcium-induced thermal gelation of pea protein and elucidated the mechanism of improved digestibility through microstructural modification. Results show that enzymatic deamidation significantly improves calcium-induced thermal gelation of pea protein isolate, reducing minimum gelation concentration from 9 % to 3 % and increasing calcium tolerance from 20 mM to 40 mM compared to native pea protein isolate (NPPI). Microstructural analysis revealed deamidated PPI (DPPI) formed homogeneous fine-stranded networks, while NPPI developed rough porous networks composed of large-sized protein aggregates. This structural transformation, attributed to increased carboxyl groups facilitating calcium bridging, enhanced gel strength, water-holding capacity, and digestive nutritional properties. The fine-stranded network structure of DPPI gels significantly improved protein digestibility (68–86 % vs. 57 %) and calcium bioavailability (85–90 % vs. 77 %) by promoting contact between digestive enzymes and protein substrates, increasing the accessibility of cleavage sites and facilitating the release of calcium-peptide complexes. Deamidation offers a promising strategy for creating pea protein gels with superior functionality and nutritional value.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"172 \",\"pages\":\"Article 111968\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-09-10\",\"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/S0268005X25009282\",\"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/S0268005X25009282","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}
Enhancement of protein gelation and nutritional properties in pea protein gels through enzymatic deamidation
Pea protein exhibits poor gelation properties due to low cysteine content, limiting its application as a structural ingredient in food systems. This study investigated the effects of enzymatic deamidation on calcium-induced thermal gelation of pea protein and elucidated the mechanism of improved digestibility through microstructural modification. Results show that enzymatic deamidation significantly improves calcium-induced thermal gelation of pea protein isolate, reducing minimum gelation concentration from 9 % to 3 % and increasing calcium tolerance from 20 mM to 40 mM compared to native pea protein isolate (NPPI). Microstructural analysis revealed deamidated PPI (DPPI) formed homogeneous fine-stranded networks, while NPPI developed rough porous networks composed of large-sized protein aggregates. This structural transformation, attributed to increased carboxyl groups facilitating calcium bridging, enhanced gel strength, water-holding capacity, and digestive nutritional properties. The fine-stranded network structure of DPPI gels significantly improved protein digestibility (68–86 % vs. 57 %) and calcium bioavailability (85–90 % vs. 77 %) by promoting contact between digestive enzymes and protein substrates, increasing the accessibility of cleavage sites and facilitating the release of calcium-peptide complexes. Deamidation offers a promising strategy for creating pea protein gels with superior functionality and nutritional value.
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.