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Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks

The gap between the current supply and future demand of meat has increased the need to produce plant-based meat analogs. Methylcellulose (MC) is used in most commercial products. Consumers and manufacturers require the development of other novel binding systems, as MC is not chemical-free. We aimed...

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Autores principales: Sakai, Kiyota, Sato, Yukihide, Okada, Masamichi, Yamaguchi, Shotaro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8370993/
https://www.ncbi.nlm.nih.gov/pubmed/34404846
http://dx.doi.org/10.1038/s41598-021-96058-4
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author Sakai, Kiyota
Sato, Yukihide
Okada, Masamichi
Yamaguchi, Shotaro
author_facet Sakai, Kiyota
Sato, Yukihide
Okada, Masamichi
Yamaguchi, Shotaro
author_sort Sakai, Kiyota
collection PubMed
description The gap between the current supply and future demand of meat has increased the need to produce plant-based meat analogs. Methylcellulose (MC) is used in most commercial products. Consumers and manufacturers require the development of other novel binding systems, as MC is not chemical-free. We aimed to develop a novel chemical-free binding system for meat analogs. First, we found that laccase (LC) synergistically crosslinks proteins and sugar beet pectin (SBP). To investigate the ability of these SBP-protein crosslinks, textured vegetable protein (TVP) was used. The presence of LC and SBP improved the moldability and binding ability of patties, regardless of the type, shape, and size of TVPs. The hardness of LC-treated patties with SBP reached 32.2 N, which was 1.7- and 7.9-fold higher than that of patties with MC and transglutaminase-treated patties. Additionally, the cooking loss and water/oil-holding capacity of LC-treated patties with SBP improved by up to 8.9–9.4% and 5.8–11.3%, compared with patties with MC. Moreover, after gastrointestinal digestion, free amino nitrogen released from LC-treated patties with SBP was 2.3-fold higher than that released from patties with MC. This is the first study to report protein-SBP crosslinks by LC as chemical-free novel binding systems for meat analogs.
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spelling pubmed-83709932021-08-19 Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks Sakai, Kiyota Sato, Yukihide Okada, Masamichi Yamaguchi, Shotaro Sci Rep Article The gap between the current supply and future demand of meat has increased the need to produce plant-based meat analogs. Methylcellulose (MC) is used in most commercial products. Consumers and manufacturers require the development of other novel binding systems, as MC is not chemical-free. We aimed to develop a novel chemical-free binding system for meat analogs. First, we found that laccase (LC) synergistically crosslinks proteins and sugar beet pectin (SBP). To investigate the ability of these SBP-protein crosslinks, textured vegetable protein (TVP) was used. The presence of LC and SBP improved the moldability and binding ability of patties, regardless of the type, shape, and size of TVPs. The hardness of LC-treated patties with SBP reached 32.2 N, which was 1.7- and 7.9-fold higher than that of patties with MC and transglutaminase-treated patties. Additionally, the cooking loss and water/oil-holding capacity of LC-treated patties with SBP improved by up to 8.9–9.4% and 5.8–11.3%, compared with patties with MC. Moreover, after gastrointestinal digestion, free amino nitrogen released from LC-treated patties with SBP was 2.3-fold higher than that released from patties with MC. This is the first study to report protein-SBP crosslinks by LC as chemical-free novel binding systems for meat analogs. Nature Publishing Group UK 2021-08-17 /pmc/articles/PMC8370993/ /pubmed/34404846 http://dx.doi.org/10.1038/s41598-021-96058-4 Text en © The Author(s) 2021 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
Sakai, Kiyota
Sato, Yukihide
Okada, Masamichi
Yamaguchi, Shotaro
Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
title Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
title_full Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
title_fullStr Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
title_full_unstemmed Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
title_short Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
title_sort improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8370993/
https://www.ncbi.nlm.nih.gov/pubmed/34404846
http://dx.doi.org/10.1038/s41598-021-96058-4
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