ArticleScientific reports2021
β-elimination of hyaluronate by red king crab hyaluronidase.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- From permeation enhancer to therapeutic enabler: Advances, applications, and translational perspectives in hyaluronidase-based drug delivery.Materials today. Bio · 2026Review
- Rational structural design for the dual enhancement of catalytic activity and thermal stability of hyaluronidase from Citrobacter portucalensis.Biotechnology for biofuels and bioproducts · 2026Article
- Hyaluronic acid degradation by Purpureocillium lilacinum: biochemical and transcriptomic insights.Applied microbiology and biotechnology · 2026Article
- Functional Analysis ofInternational journal of molecular sciences · 2025Article
- Novel Antimicrobial Peptide from the Hepatopancreas of the Red King Crab.International journal of molecular sciences · 2023Article
- Interactions between Nitric Oxide and Hyaluronan Implicate the Migration of Breast Cancer Cells.Biomacromolecules · 2022Article
- Investigation of lipolytic activity of the red king crab hepatopancreas homogenate by NMR spectroscopy.PeerJ · 2022Article
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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 [Formula: see text]-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.
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