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

Abstract 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....

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Autores principales:	Kiyota Sakai, Yukihide Sato, Masamichi Okada, Shotaro Yamaguchi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/32adf795f65a498198f21321c53a01f2
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spelling	oai:doaj.org-article:32adf795f65a498198f21321c53a01f22021-12-02T17:08:36ZImproved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks10.1038/s41598-021-96058-42045-2322https://doaj.org/article/32adf795f65a498198f21321c53a01f22021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-96058-4https://doaj.org/toc/2045-2322Abstract 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.Kiyota SakaiYukihide SatoMasamichi OkadaShotaro YamaguchiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kiyota Sakai Yukihide Sato Masamichi Okada Shotaro Yamaguchi Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
description	Abstract 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.
format	article
author	Kiyota Sakai Yukihide Sato Masamichi Okada Shotaro Yamaguchi
author_facet	Kiyota Sakai Yukihide Sato Masamichi Okada Shotaro Yamaguchi
author_sort	Kiyota Sakai
title	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_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_sort	improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/32adf795f65a498198f21321c53a01f2
work_keys_str_mv	AT kiyotasakai improvedfunctionalpropertiesofmeatanalogsbylaccasecatalyzedproteinandpectincrosslinks AT yukihidesato improvedfunctionalpropertiesofmeatanalogsbylaccasecatalyzedproteinandpectincrosslinks AT masamichiokada improvedfunctionalpropertiesofmeatanalogsbylaccasecatalyzedproteinandpectincrosslinks AT shotaroyamaguchi improvedfunctionalpropertiesofmeatanalogsbylaccasecatalyzedproteinandpectincrosslinks
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Improved functional properties of meat analogs by laccase catalyzed protein and pectin crosslinks

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