Development of a New Type of Recombinant Hyaluronidase Using a Hexahistidine; Possibilities and Challenges in Commercialization
| Autor: | Bong-Seok Song, Sang-Hyun Kim, Sang-Rae Lee, Tae-Kil Eom, Yena Jung, Young-Ho Park, Yun-Kyoung Song, Ju-Sung Kim, Chaeri Park, Young-Hyun Kim, Ji-Su Kim, Ekyune Kim, Sun-Uk Kim |
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| Rok vydání: | 2019 |
| Předmět: |
Hyaluronoglucosaminidase
Applied Microbiology and Biotechnology law.invention chemistry.chemical_compound Affinity chromatography Hyaluronidase law Enzyme Stability Hyaluronic acid medicine Animals Humans Histidine Cloning Molecular Hyaluronic Acid Drug transport chemistry.chemical_classification Temperature General Medicine Hydrogen-Ion Concentration Recombinant Proteins HEK293 Cells Enzyme chemistry Biochemistry Recombinant DNA Capillary vessels Cattle Cell Adhesion Molecules Oligopeptides Biotechnology medicine.drug |
| Zdroj: | Journal of Microbiology and Biotechnology. 29:1310-1315 |
| ISSN: | 1738-8872 1017-7825 |
| Popis: | Hyaluronidases enhance therapeutic drug transport by breaking down the hyaluronan barrier to lymphatic and capillary vessels, facilitating their tissue absorption. Commercially available hyaluronidases are bovine in origin; however, they pose risks such as bovine spongiform encephalopathy. The present study aimed to develop a novel, highly active hyaluronidase and assess its function. Therefore, in order to find the most efficient active hyaluronidase, we produced several shortened hyaluronidases with partial removal of the N- or C-terminal regions. Moreover, we created an enzyme that connected six histidines onto the end of the hyaluronidase C-terminus. This simplified subsequent purification using Ni2+ affinity chromatography, making it feasible to industrialize this highly active recombinant hyaluronidase which exhibited catalytic activity equal to that of the commercial enzyme. Therefore, this simple and effective isolation method could increase the availability of recombinant hyaluronidase for research and clinical purposes. |
| Databáze: | OpenAIRE |
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