journal article·2019

Horseradish peroxidase-catalyzed hydrogelation consuming enzyme-produced hydrogen peroxide in the presence of reducing sugars

Enkhtuul Gantumur, Shinji Sakai, Masaki Nakahata, Masahito Taya

Soft Matter· Volume 15· Issue 10
Publisher page

Abstract

In the present work, three kinds of reducing sugars: glucose, galactose, and mannose, are applied to horseradish peroxidase (HRP)-catalyzed hydrogelation of an aqueous solution containing natural polymers modified with phenolic hydroxyl moieties. In this system, HRP consumes hydrogen peroxide that was generated from the oxidation of thiol groups in HRP in the presence of reducing sugars. Herein, we highlight the versatility of applicable sugar types and the controllable hydrogel properties. The mechanical properties and microstructures of the resultant hydrogels can be well controlled by varying the concentration and the reducing power of sugars. Moreover, reducing sugar-independent cytocompatibility of the hydrogels was confirmed by the growth of cells on them. The wide selection of sugar types provides a better understanding of the reaction mechanism and enables the characterization of hydrogels with well-controlled properties.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Hydrogels: synthesis, properties, applications · Supramolecular Self-Assembly in Materials · Electrospun Nanofibers in Biomedical Applications

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Division of Chemical Engineering

Department of Materials Engineering Science

Graduate School of Engineering Science

Osaka University

Toyonaka

Funding

Japan Society for the Promotion of Science

References (32)

Show source-provided references
1. Ahmed · J. Adv. Res. · 2015 · 6 · 10510.1016/j.jare.2013.07.006 ↗
2. Jeong · J. Polym. Res. · 2017 · 24 · 11210.1007/s10965-017-1278-4 ↗
3. Kamoun · J. Adv. Res. · 2017 · 8 · 21710.1016/j.jare.2017.01.005 ↗
4. Annabi · Adv. Mater. · 2014 · 26 · 8510.1002/adma.201303233 ↗
5. Hennink · Adv. Drug Delivery Rev. · 2012 · 64 · 22310.1016/j.addr.2012.09.009 ↗
6. Raza · Pharmaceutics · 2018 · 10 · 1610.3390/pharmaceutics10010016 ↗
7. Nguyen · Eur. Polym. J. · 2015 · 72 · 60210.1016/j.eurpolymj.2015.03.016 ↗
8. Lee · Biomed. Mater. · 2015 · 11 · 01410110.1088/1748-6041/11/1/014101 ↗
9. Kurisawa · Chem. Commun. · 2005 · 431210.1039/b506989k ↗
10. Sakai · Biomacromolecules · 2007 · 8 · 262210.1021/bm070300+ ↗
11. Sakai · Biomaterials · 2009 · 30 · 337110.1016/j.biomaterials.2009.03.030 ↗
12. Moriyama · Biochem. Eng. J. · 2013 · 76 · 3710.1016/j.bej.2013.04.007 ↗
13. Sakai · J. Mater. Chem. B · 2013 · 1 · 506710.1039/c3tb20780c ↗
14. Sakai · Chem. – Asian J. · 2017 · 12 · 309810.1002/asia.201701364 ↗
15. Wefers · J. Free Radicals Biol. Med. · 1985 · 1 · 31110.1016/0748-5514(85)90137-0 ↗
16. Osswald · Free Radical Res. Commun. · 2009 · 5 · 25910.3109/10715768909074709 ↗
17. Singh · Angew. Chem., Int. Ed. Engl. · 2013 · 52 · 300010.1002/anie.201206266 ↗
18. Moriyama · Chem. Commun. · 2014 · 50 · 589510.1039/C3CC49766F ↗
19. Moriyama · Biotechnol. J. · 2016 · 11 · 145210.1002/biot.201600087 ↗
20. Mishina · Biomacromolecules · 2016 · 17 · 197810.1021/acs.biomac.6b00149 ↗
21. Gantumur · ACS Macro Lett. · 2017 · 6 · 48510.1021/acsmacrolett.7b00122 ↗
22. Bindoli · Antioxid. Redox Signaling · 2008 · 10 · 154910.1089/ars.2008.2063 ↗
23. Barbara · J. Biol. Chem. · 1997 · 272 · 2031310.1074/jbc.272.33.20313 ↗
24. Sakai · Acta Biomater. · 2007 · 3 · 49510.1016/j.actbio.2006.12.002 ↗
25. Ellman · Arch. Biochem. Biophys. · 1959 · 82 · 7010.1016/0003-9861(59)90090-6 ↗
26. Branco · Biomaterials · 2009 · 30 · 133910.1016/j.biomaterials.2008.11.019 ↗
27. Bekeschus · Free Radical Res. · 2014 · 48 · 54210.3109/10715762.2014.892937 ↗
28. Strickland · Biochem. Biophys. Acta Enzymol. · 1968 · 151 · 7010.1016/0005-2744(68)90162-9 ↗
29. Akita · Biosci. Biotecnol. Biochem. · 2001 · 65 · 158110.1271/bbb.65.1581 ↗
30. Ryu · Biochemistry · 1992 · 31 · 258810.1021/bi00124a020 ↗
31. Hatanaka · Agric. Biol. Chem. · 1980 · 44 · 2943
32. Wang · Acta Biomater. · 2012 · 8 · 51910.1016/j.actbio.2011.09.030 ↗