Radiofrequency treatment enhances the catalytic function of an immobilized nanobiohybrid catalyst
Source abstract
Abstract
Biocatalysis, the use of enzymes in chemical transformation, has undergone intensive development for a wide range of applications. As such, maximizing the functionality of enzymes for biocatalysis is a major priority to enable industrial use. To date, many innovative technologies have been developed to address the future demand of enzymes for these purposes, but maximizing the catalytic activity of enzymes remains a challenge. In this study, we demonstrated that the functionality of a nanobiocatalyst could be enhanced by combining immobilization and radiofrequency (RF) treatment. Aminopeptidase PepA-encapsulating 2 nm platinum nanoparticles (PepA-PtNPs) with the catalytic activities of hydrolysis and hydrogenation were employed as multifunctional nanobiocatalysts. Immobilizing the nanobiocatalysts in a hydrogel using metal chelation significantly enhanced their functionalities, including catalytic power, thermal-stability, pH tolerance, organic solvent tolerance, and reusability. Most importantly, RF treatment of the hydrogel-immobilized PepA-PtNPs increased their catalytic power by 2.5 fold greater than the immobilized PepA. Our findings indicate that the catalytic activities and functionalities of PepA-PtNPs are greatly enhanced by the combination of hydrogel-immobilization and RF treatment. Based on our findings, we propose that RF treatment of nanobiohybrid catalysts immobilized on the bulk hydrogel represents a new strategy for achieving efficient biocatalysis.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Enzyme Catalysis and Immobilization · Electrochemical sensors and biosensors · Peptidase Inhibition and Analysis
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Sungkyunkwan Advanced Institute of Nanotechnology (SAINT)
Sungkyunkwan University
Suwon 440-746, Korea
Department of Molecular Cell Biology
Samsung Biomedical Research Institute
Department of Polymer Science and Engineering
Pusan National University
Busan 609-735, Korea
References (47)
Show source-provided references
1. Schoemaker · Science · 2003 · 299 · 169410.1126/science.1079237 ↗
2. Schmid · Nature · 2001 · 409 · 25810.1038/35051736 ↗
3. Bornscheuer · Nature · 2012 · 485 · 18510.1038/nature11117 ↗
4. Brady · Biotechnol. Lett. · 2009 · 31 · 163910.1007/s10529-009-0076-4 ↗
5. Le Goff · Science · 2009 · 326 · 138410.1126/science.1179773 ↗
6. Rozhkova · Nano Lett. · 2009 · 9 · 333710.1021/nl901610f ↗
7. Lin · Biomaterials · 2013 · 34 · 260010.1016/j.biomaterials.2013.01.007 ↗
8. Song · Adv. Mater. · 2010 · 22 · 220610.1002/adma.200903783 ↗
9. Tang · Anal. Chem. · 2011 · 83 · 861110.1021/ac202049q ↗
10. Xu · Adv. Funct. Mater. · 2014 · 24 · 162410.1002/adfm.201301649 ↗
11. Lin · Acc. Chem. Res. · 2014 · 47 · 109710.1021/ar400250z ↗
12. San · Angew. Chem., Int. Ed. · 2011 · 50 · 1192410.1002/anie.201101833 ↗
13. San · J. Mater. Chem. · 2012 · 22 · 177410.1039/C1JM14581A ↗
14. Hartmann · J. Mater. Chem. · 2010 · 20 · 84410.1039/B907869J ↗
15. Mahmoud · J. Appl. Polym. Sci. · 2009 · 5 · 2466
16. Cao · Curr. Opin. Chem. Biol. · 2005 · 9 · 21710.1016/j.cbpa.2005.02.014 ↗
17. L. Cao , Introduction: Immobilized Enzymes: Past, Present and Prospects , in Carrier-bound Immobilized Enzymes , Wiley-VCH Verlag GmbH & Co. KGaA , 2006 , pp. 1–52
18. Jang · Polym. Adv. Technol. · 2010 · 21 · 47610.1002/pat.1455 ↗
19. Wang · Curr. Opin. Biotechnol. · 2006 · 17 · 57410.1016/j.copbio.2006.10.009 ↗
20. Kara · React. Funct. Polym. · 2005 · 62 · 6110.1016/j.reactfunctpolym.2004.08.008 ↗
21. Peppas · Adv. Mater. · 2006 · 18 · 134510.1002/adma.200501612 ↗
22. Basri · J. Appl. Polym. Sci. · 2001 · 82 · 140410.1002/app.1977 ↗
23. Chauhan · J. Appl. Polym. Sci. · 2004 · 92 · 313510.1002/app.20244 ↗
24. Betigeri · Biomaterials · 2002 · 23 · 362710.1016/S0142-9612(02)00095-9 ↗
25. Kanwar · J. Appl. Polym. Sci. · 2006 · 100 · 463610.1002/app.23129 ↗
26. Pekel · J. Biomater. Sci., Polym. Ed. · 2005 · 16 · 25310.1163/1568562053115453 ↗
27. Ha · J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. · 2008 · 876 · 810.1016/j.jchromb.2008.10.020 ↗
28. Ha · Polym. Adv. Technol. · 2013 · 24 · 7510.1002/pat.3052 ↗
29. Ha · Macromol. Res. · 2013 · 21 · 510.1007/s13233-013-1007-8 ↗
30. Piyasena · Crit. Rev. Food Sci. Nutr. · 2003 · 43 · 58710.1080/10408690390251129 ↗
31. Wang · Biosystems Engineering · 2003 · 85 · 20110.1016/S1537-5110(03)00042-4 ↗
32. Raoof · Int. J. Hepatol. · 2011 · 2011 · 67695710.4061/2011/676957 ↗
33. Kruse · IEEE Trans. Biomed. Eng. · 2011 · 58 · 200210.1109/TBME.2011.2124460 ↗
34. Dutta · Bioelectromagnetics · 1992 · 13 · 31710.1002/bem.2250130407 ↗
35. Kim · Biochem. Biophys. Res. Commun. · 2010 · 391 · 43110.1016/j.bbrc.2009.11.075 ↗
36. San · J. Mater. Chem. B · 2013 · 1 · 145310.1039/c2tb00290f ↗
37. Bradford · Anal. Biochem. · 1976 · 72 · 24810.1016/0003-2697(76)90527-3 ↗
38. Xiao · J. Am. Chem. Soc. · 2007 · 129 · 961010.1021/ja072344w ↗
39. Kim · Catal. Commun. · 2009 · 10 · 130510.1016/j.catcom.2009.02.013 ↗
40. San · Int. J. Hyperthermia · 2013 · 29 · 9910.3109/02656736.2012.760137 ↗
41. Roy · Enzyme Microb. Technol. · 2001 · 29 · 49010.1016/S0141-0229(01)00425-2 ↗
42. Klibanov · Nature · 2001 · 409 · 24110.1038/35051719 ↗
43. Hong · Appl. Microbiol. Biotechnol. · 2006 · 73 · 8010.1007/s00253-006-0428-0 ↗
44. Wang · Chem. Commun. · 2007 · 103210.1039/b615223f ↗
45. Hasche · Phys. Chem. Chem. Phys. · 2010 · 12 · 1525110.1039/c0cp00609b ↗
46. Hasche · ChemCatChem · 2011 · 3 · 180510.1002/cctc.201100169 ↗
47. H. Zhao , Chapter 5 Microwave-assisted Enzymatic Reactions in Aqueous Media , in Aqueous Microwave Assisted Chemistry , The Royal Society of Chemistry , 2010 , pp. 123–144