{"title":"Gelation behavior of lentil protein aggregates induced by sequential combination of glucono-δ-lactone and transglutaminase","authors":"Yeon-Ji Jo , Lingyun Chen","doi":"10.1016/j.foostr.2023.100312","DOIUrl":null,"url":null,"abstract":"<div><p>This study introduces a cold-set lentil protein (LP) gel with significantly improved mechanical strength prepared from protein fibrillar aggregates. First, fibrillar aggregates were formed by thermal treatment at an alkaline pH. Subsequently, glucono-δ-lactone (GDL), transglutaminase (TG), or their sequential combination (GDL/TG) was applied to induce the gelation<span> of LP aggregates at room temperature. The gelling mechanism study revealed the formation of covalent bonds in the gel network induced by TG, which was then reinforced by hydrophobic interactions among the protein aggregates induced by GDL. As expected, the sequentially addition of TG and GDL enabled formation of interconnected networks with thick walls and significantly improved gel hardness. This research has provided a new strategy to develop strong lentil protein gels for food texturization thus potentially expanding food applications of lentil protein as an advantageous plant source of protein.</span></p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"36 ","pages":"Article 100312"},"PeriodicalIF":5.6000,"publicationDate":"2023-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Structure-Netherlands","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2213329123000059","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 2
Abstract
This study introduces a cold-set lentil protein (LP) gel with significantly improved mechanical strength prepared from protein fibrillar aggregates. First, fibrillar aggregates were formed by thermal treatment at an alkaline pH. Subsequently, glucono-δ-lactone (GDL), transglutaminase (TG), or their sequential combination (GDL/TG) was applied to induce the gelation of LP aggregates at room temperature. The gelling mechanism study revealed the formation of covalent bonds in the gel network induced by TG, which was then reinforced by hydrophobic interactions among the protein aggregates induced by GDL. As expected, the sequentially addition of TG and GDL enabled formation of interconnected networks with thick walls and significantly improved gel hardness. This research has provided a new strategy to develop strong lentil protein gels for food texturization thus potentially expanding food applications of lentil protein as an advantageous plant source of protein.
期刊介绍：
Food Structure is the premier international forum devoted to the publication of high-quality original research on food structure. The focus of this journal is on food structure in the context of its relationship with molecular composition, processing and macroscopic properties (e.g., shelf stability, sensory properties, etc.). Manuscripts that only report qualitative findings and micrographs and that lack sound hypothesis-driven, quantitative structure-function research are not accepted. Significance of the research findings for the food science community and/or industry must also be highlighted.
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