β-elimination of hyaluronate by red king crab hyaluronidase

Abstract Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its com...

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Autores principales:	Dmitrii Sliadovskii, Tatyana Ponomareva, Maxim Molchanov, Irina Pozdnyakova-Filatova, Maria Timchenko, Victor Marchenkov, Oleg Gusev, Evgeny Sogorin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a6d32574c3b84934b4ac0d27507d6226
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spelling	oai:doaj.org-article:a6d32574c3b84934b4ac0d27507d62262021-11-21T12:19:32Zβ-elimination of hyaluronate by red king crab hyaluronidase10.1038/s41598-021-01890-32045-2322https://doaj.org/article/a6d32574c3b84934b4ac0d27507d62262021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-01890-3https://doaj.org/toc/2045-2322Abstract Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial counterpart. Zymography revealed that the molecular weight of a protein with hyalorunidase activity is 40–50 kDa. Analysis of the hepatopancreas transcriptome and results of cloning and sequencing of cDNA revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. Further analysis showed that hyaluronat enzymatic cleavage follows the $$\beta $$ β -elimination mechanism, which is well known for bacterial hyaluronidases. The results of ion-exchange chromatography showed that the final product of hyaluronate degradation is unsaturated tetrasaccharide. Thus, we identified a new hyaluronidase of higher eukaryotes, which is not integrated into the modern classification of hyaluronidases.Dmitrii SliadovskiiTatyana PonomarevaMaxim MolchanovIrina Pozdnyakova-FilatovaMaria TimchenkoVictor MarchenkovOleg GusevEvgeny SogorinNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Dmitrii Sliadovskii Tatyana Ponomareva Maxim Molchanov Irina Pozdnyakova-Filatova Maria Timchenko Victor Marchenkov Oleg Gusev Evgeny Sogorin β-elimination of hyaluronate by red king crab hyaluronidase
description	Abstract Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial counterpart. Zymography revealed that the molecular weight of a protein with hyalorunidase activity is 40–50 kDa. Analysis of the hepatopancreas transcriptome and results of cloning and sequencing of cDNA revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. Further analysis showed that hyaluronat enzymatic cleavage follows the $$\beta $$ β -elimination mechanism, which is well known for bacterial hyaluronidases. The results of ion-exchange chromatography showed that the final product of hyaluronate degradation is unsaturated tetrasaccharide. Thus, we identified a new hyaluronidase of higher eukaryotes, which is not integrated into the modern classification of hyaluronidases.
format	article
author	Dmitrii Sliadovskii Tatyana Ponomareva Maxim Molchanov Irina Pozdnyakova-Filatova Maria Timchenko Victor Marchenkov Oleg Gusev Evgeny Sogorin
author_facet	Dmitrii Sliadovskii Tatyana Ponomareva Maxim Molchanov Irina Pozdnyakova-Filatova Maria Timchenko Victor Marchenkov Oleg Gusev Evgeny Sogorin
author_sort	Dmitrii Sliadovskii
title	β-elimination of hyaluronate by red king crab hyaluronidase
title_short	β-elimination of hyaluronate by red king crab hyaluronidase
title_full	β-elimination of hyaluronate by red king crab hyaluronidase
title_fullStr	β-elimination of hyaluronate by red king crab hyaluronidase
title_full_unstemmed	β-elimination of hyaluronate by red king crab hyaluronidase
title_sort	β-elimination of hyaluronate by red king crab hyaluronidase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/a6d32574c3b84934b4ac0d27507d6226
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β-elimination of hyaluronate by red king crab hyaluronidase

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