Loes J. G. Hoppenreijs, Sarah E. Brune, Rebekka Biedendieck, Rainer Krull, Remko M. Boom, Julia K. Keppler
{"title":"Exploring Functionality Gain for (Recombinant) β-Lactoglobulin Through Production and Processing Interventions","authors":"Loes J. G. Hoppenreijs, Sarah E. Brune, Rebekka Biedendieck, Rainer Krull, Remko M. Boom, Julia K. Keppler","doi":"10.1007/s11947-024-03414-z","DOIUrl":null,"url":null,"abstract":"<p>Interventions in the upstream production and further processing of recombinant food proteins affect its properties when used for food application. Often the efficiency of particular interventions is evaluated based on molecular purity and yield rather than final functional properties. Yet, the formulation of foods, including the amount of protein required, can be affected when the functional properties have changed. In this explorative study, we exemplify how far we can extend the functionality range of the major whey protein β-lactoglobulin (BLG), in terms of foaming and (heat-set) gelling, through various interventions. Slight changes in the amino acid sequence of BLG affected its functional properties significantly. Foams were up to ten times more stable, when selecting different natural isoforms of BLG (isoform A instead of B) or when inducing targeted cysteine mutations. The isoform B yielded stronger thermally induced gels (+ 40%) compared to isoform A. During downstream processing of recombinantly secreted BLG, limited purification of up to ~ 67 wt% enabled reasonable foaming properties and superior gelation, while a lower purity of ~ 22 wt% resulted in poor performance in both cases. Post-processing allowed conversion of native whey protein into soluble amyloid-like aggregates. These aggregates resulted in better foam stability (i.e., approximately four times longer than non-aggregated protein), but did not improve gelation. The presented study demonstrates that one should consider not only protein yield and purity, but also functional properties when developing recombinant proteins for food application. In turn, these functional properties are a result of the complete upstream and downstream chain.</p>","PeriodicalId":562,"journal":{"name":"Food and Bioprocess Technology","volume":null,"pages":null},"PeriodicalIF":5.3000,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food and Bioprocess Technology","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1007/s11947-024-03414-z","RegionNum":2,"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: 0
Abstract
Interventions in the upstream production and further processing of recombinant food proteins affect its properties when used for food application. Often the efficiency of particular interventions is evaluated based on molecular purity and yield rather than final functional properties. Yet, the formulation of foods, including the amount of protein required, can be affected when the functional properties have changed. In this explorative study, we exemplify how far we can extend the functionality range of the major whey protein β-lactoglobulin (BLG), in terms of foaming and (heat-set) gelling, through various interventions. Slight changes in the amino acid sequence of BLG affected its functional properties significantly. Foams were up to ten times more stable, when selecting different natural isoforms of BLG (isoform A instead of B) or when inducing targeted cysteine mutations. The isoform B yielded stronger thermally induced gels (+ 40%) compared to isoform A. During downstream processing of recombinantly secreted BLG, limited purification of up to ~ 67 wt% enabled reasonable foaming properties and superior gelation, while a lower purity of ~ 22 wt% resulted in poor performance in both cases. Post-processing allowed conversion of native whey protein into soluble amyloid-like aggregates. These aggregates resulted in better foam stability (i.e., approximately four times longer than non-aggregated protein), but did not improve gelation. The presented study demonstrates that one should consider not only protein yield and purity, but also functional properties when developing recombinant proteins for food application. In turn, these functional properties are a result of the complete upstream and downstream chain.
期刊介绍:
Food and Bioprocess Technology provides an effective and timely platform for cutting-edge high quality original papers in the engineering and science of all types of food processing technologies, from the original food supply source to the consumer’s dinner table. It aims to be a leading international journal for the multidisciplinary agri-food research community.
The journal focuses especially on experimental or theoretical research findings that have the potential for helping the agri-food industry to improve process efficiency, enhance product quality and, extend shelf-life of fresh and processed agri-food products. The editors present critical reviews on new perspectives to established processes, innovative and emerging technologies, and trends and future research in food and bioproducts processing. The journal also publishes short communications for rapidly disseminating preliminary results, letters to the Editor on recent developments and controversy, and book reviews.