Developing thermally stable beverage emulsions using mildly fractionated pea proteins

IF 1.9 4区 农林科学 Q3 CHEMISTRY, APPLIED
Neksha Diwakar Devaki, Supratim Ghosh
{"title":"Developing thermally stable beverage emulsions using mildly fractionated pea proteins","authors":"Neksha Diwakar Devaki,&nbsp;Supratim Ghosh","doi":"10.1002/aocs.12825","DOIUrl":null,"url":null,"abstract":"<p>Oil-in-water emulsions are widely used as the base flavoring or clouding agents in various beverages. Pulse proteins can play a major role as a natural emulsifier in beverages. However, the presence of insoluble components greatly minimizes their potential application in beverage emulsions. In this work, pea protein concentrate was mildly fractionated by aqueous centrifugation to recover a soluble fraction with 71% protein yield, which was then used to develop 5% oil-in-water emulsions using a high-pressure homogenizer. Emulsion stability was tested by heat treatment (90°C, 30 min) in the presence of NaCl (0–1 M) at pH 7.0 and 2.0. Stability increased upon the addition of salt at pH 7, while at pH 2, proteins and droplets aggregated. Heat treatment led to extensive aggregation at both pH values, which was further worsened by salt. To prevent thermal destabilization, the proteins were heat-treated at 75°C for 30 min for partial denaturation before emulsification under hot conditions. The heat-treated protein-stabilized emulsions at pH 7 had superior thermal stability at all salt concentrations without aggregation. However, a similar improvement was not observed at pH 2. Pre-heating the soluble protein exposed the hydrophobic patches, leading to better adsorption on the droplet surface, which did not show additional aggregation upon further heating the emulsions at pH 7. Interestingly, heat-treated protein-stabilized emulsions showed a 44% drop in lipid digestibility compared to the original emulsions. The proposed approach could be a valuable addition to the utilization of pea proteins in beverage emulsions that could withstand heat treatment during food processing.</p>","PeriodicalId":17182,"journal":{"name":"Journal of the American Oil Chemists Society","volume":"101 10","pages":"981-996"},"PeriodicalIF":1.9000,"publicationDate":"2024-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the American Oil Chemists Society","FirstCategoryId":"97","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/aocs.12825","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0

Abstract

Oil-in-water emulsions are widely used as the base flavoring or clouding agents in various beverages. Pulse proteins can play a major role as a natural emulsifier in beverages. However, the presence of insoluble components greatly minimizes their potential application in beverage emulsions. In this work, pea protein concentrate was mildly fractionated by aqueous centrifugation to recover a soluble fraction with 71% protein yield, which was then used to develop 5% oil-in-water emulsions using a high-pressure homogenizer. Emulsion stability was tested by heat treatment (90°C, 30 min) in the presence of NaCl (0–1 M) at pH 7.0 and 2.0. Stability increased upon the addition of salt at pH 7, while at pH 2, proteins and droplets aggregated. Heat treatment led to extensive aggregation at both pH values, which was further worsened by salt. To prevent thermal destabilization, the proteins were heat-treated at 75°C for 30 min for partial denaturation before emulsification under hot conditions. The heat-treated protein-stabilized emulsions at pH 7 had superior thermal stability at all salt concentrations without aggregation. However, a similar improvement was not observed at pH 2. Pre-heating the soluble protein exposed the hydrophobic patches, leading to better adsorption on the droplet surface, which did not show additional aggregation upon further heating the emulsions at pH 7. Interestingly, heat-treated protein-stabilized emulsions showed a 44% drop in lipid digestibility compared to the original emulsions. The proposed approach could be a valuable addition to the utilization of pea proteins in beverage emulsions that could withstand heat treatment during food processing.

利用温和分馏的豌豆蛋白开发热稳定饮料乳剂
水包油乳剂被广泛用作各种饮料的基础调味剂或起云剂。脉动蛋白可作为天然乳化剂在饮料中发挥重要作用。然而,不溶性成分的存在大大降低了其在饮料乳剂中的应用潜力。在这项研究中,豌豆蛋白浓缩物通过水离心法进行轻度分馏,回收了蛋白质产量为 71% 的可溶部分,然后利用高压均质机将其用于开发 5% 水包油型乳液。通过在 pH 值为 7.0 和 2.0 的 NaCl(0-1 M)存在下进行热处理(90°C,30 分钟)来测试乳液的稳定性。在 pH 值为 7 时,加入盐后稳定性增加,而在 pH 值为 2 时,蛋白质和液滴聚集。在两种 pH 值下,热处理都会导致广泛的聚集,而盐会进一步加剧这种现象。为防止热失稳,在热条件下乳化之前,先将蛋白质在 75°C 下热处理 30 分钟,使其部分变性。在 pH 值为 7 的条件下,经过热处理的蛋白质稳定乳液在所有盐浓度下都具有极佳的热稳定性,且不会出现聚集现象。预热可溶性蛋白质使疏水斑块暴露出来,从而更好地吸附在液滴表面,在 pH 值为 7 的条件下进一步加热乳剂时,液滴表面没有出现更多的聚集现象。所提出的方法可以为饮料乳液中豌豆蛋白的利用提供宝贵的补充,这种乳液可以在食品加工过程中经受住热处理。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
CiteScore
4.10
自引率
5.00%
发文量
95
审稿时长
2.4 months
期刊介绍: The Journal of the American Oil Chemists’ Society (JAOCS) is an international peer-reviewed journal that publishes significant original scientific research and technological advances on fats, oils, oilseed proteins, and related materials through original research articles, invited reviews, short communications, and letters to the editor. We seek to publish reports that will significantly advance scientific understanding through hypothesis driven research, innovations, and important new information pertaining to analysis, properties, processing, products, and applications of these food and industrial resources. Breakthroughs in food science and technology, biotechnology (including genomics, biomechanisms, biocatalysis and bioprocessing), and industrial products and applications are particularly appropriate. JAOCS also considers reports on the lipid composition of new, unique, and traditional sources of lipids that definitively address a research hypothesis and advances scientific understanding. However, the genus and species of the source must be verified by appropriate means of classification. In addition, the GPS location of the harvested materials and seed or vegetative samples should be deposited in an accredited germplasm repository. Compositional data suitable for Original Research Articles must embody replicated estimate of tissue constituents, such as oil, protein, carbohydrate, fatty acid, phospholipid, tocopherol, sterol, and carotenoid compositions. Other components unique to the specific plant or animal source may be reported. Furthermore, lipid composition papers should incorporate elements of year­to­year, environmental, and/ or cultivar variations through use of appropriate statistical analyses.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信