L-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment

This work attempts to investigate the inhibitory effect of L-lysine (Lys) on the thermal aggregation of coconut protein (CP). The results showed that under neutral conditions (pH = 7), temperature reduced the solubility and enhanced the thermally induced gel formation of CP. In addition, Lys reduced...

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Detalles Bibliográficos
Autores principales: Wang, Liqiang, Zhang, Youbang, Li, Run, Xiang, Dong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10432461/
https://www.ncbi.nlm.nih.gov/pubmed/37587151
http://dx.doi.org/10.1038/s41598-023-38758-7
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author Wang, Liqiang
Zhang, Youbang
Li, Run
Xiang, Dong
author_facet Wang, Liqiang
Zhang, Youbang
Li, Run
Xiang, Dong
author_sort Wang, Liqiang
collection PubMed
description This work attempts to investigate the inhibitory effect of L-lysine (Lys) on the thermal aggregation of coconut protein (CP). The results showed that under neutral conditions (pH = 7), temperature reduced the solubility and enhanced the thermally induced gel formation of CP. In addition, Lys reduced the fluorescence properties, particle size and increased the turbidity of CP, which had an inhibitory effect on heat induced gels. The results indicate that Lys plays an important role in inhibiting protein thermal aggregation by interacting with CP to create steric hindrance and increase protein electrostatic repulsion.
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spelling pubmed-104324612023-08-18 L-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment Wang, Liqiang Zhang, Youbang Li, Run Xiang, Dong Sci Rep Article This work attempts to investigate the inhibitory effect of L-lysine (Lys) on the thermal aggregation of coconut protein (CP). The results showed that under neutral conditions (pH = 7), temperature reduced the solubility and enhanced the thermally induced gel formation of CP. In addition, Lys reduced the fluorescence properties, particle size and increased the turbidity of CP, which had an inhibitory effect on heat induced gels. The results indicate that Lys plays an important role in inhibiting protein thermal aggregation by interacting with CP to create steric hindrance and increase protein electrostatic repulsion. Nature Publishing Group UK 2023-08-16 /pmc/articles/PMC10432461/ /pubmed/37587151 http://dx.doi.org/10.1038/s41598-023-38758-7 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Wang, Liqiang
Zhang, Youbang
Li, Run
Xiang, Dong
L-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment
title L-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment
title_full L-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment
title_fullStr L-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment
title_full_unstemmed L-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment
title_short L-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment
title_sort l-lysine moderates thermal aggregation of coconut proteins induced by thermal treatment
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10432461/
https://www.ncbi.nlm.nih.gov/pubmed/37587151
http://dx.doi.org/10.1038/s41598-023-38758-7
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AT lirun llysinemoderatesthermalaggregationofcoconutproteinsinducedbythermaltreatment
AT xiangdong llysinemoderatesthermalaggregationofcoconutproteinsinducedbythermaltreatment

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