{"title":"Developing thermally stable beverage emulsions using mildly fractionated pea proteins","authors":"Neksha Diwakar Devaki, 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":null,"pages":null},"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.
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.