journal article·2019-07

Nonhydrolytic sol–gel synthesized oligosiloxane resin reinforced thiol-ene photocured coatings for the immobilization of acetylcholinesterase

Emrah Çakmakçi, Serap Demir

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Abstract

Acetylcholinesterase (AChE), which is responsible for the hydrolysis of neurotransmitter acetylcholine, is a critical enzyme for the nervous system and also a biomarker for organophosphorous pesticide detection. The immobilization of AChE is an active area of research and recently the use of sol–gel-derived materials for enzyme immobilization has gained a lot of attraction. In this work, AChE was covalently immobilized onto a photocured substrate which was reinforced with an oligosiloxane resin. The oligosiloxane resin was designed to have both vinyl and epoxide groups and prepared via nonhydrolytic sol–gel technique. The strategy employed in this study offered a platform that has good mechanical and thermal properties and also suitable for modification. Thus, AChE was also immobilized onto these substrates after amine modification of the epoxy groups and followed by glutaraldehyde activation. Over 80% enzyme immobilization yield was achieved. At certain pH values (5.5 and 8.5) and under relatively higher temperatures (above 40 °C) the immobilized enzymes were found to have higher catalytic activity than the free enzyme. Furthermore, by immobilization the reuse and the storage stability of the enzyme was improved and the stability of the immobilized enzyme against the inhibitory effects of certain metal cations was enhanced.
Source: openaire · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Cholinesterase and Neurodegenerative Diseases · Electrochemical sensors and biosensors · Chemical Synthesis and Reactions

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

References (43)

Show source-provided references
1. Quinn DM (1987) Chem Rev 87:955–97910.1021/cr00081a005 ↗
2. Monton MRN, Lebert JM, Little JRL, Nair JJ, McNulty J, Brennan JD (2010) Anal Chem 82:9365–937310.1021/ac101949s ↗
3. Haque R, Nazir A (2017) In: Grover A (ed) Drug design: principles and applications, Springer, Singapore.
4. Diao J, Yu X, Ma L, Li Y, Sun Y (2018) Bioconjugate Chem 29:1703–171310.1021/acs.bioconjchem.8b00160 ↗
5. Colovic MB, Krstic DZ, Lazarevi-Pasti TD, Bondzic AM, Vasic VM (2013) Curr Neuropharmacol 11:315–33510.2174/1570159X11311030006 ↗
6. Cancar HD, Soylemez S, Akpinar Y, Kesik M, Göker S, Gunbas G, Volkan M, Toppare L (2016) ACS Appl Mater Interfaces 8:8058–806710.1021/acsami.5b12383 ↗
7. Dwevedi A (2016) Enzyme Immobilization Advances in Industry, Agriculture, Medicine, and the Environment. Springer, Switzerland10.1007/978-3-319-41418-8 ↗
8. Türünç O, Kahraman MV, Akdemir ZS, Kayaman-Apohan N, Güngör A (2009) Food Chem 112:992–99710.1016/j.foodchem.2008.07.024 ↗
9. Reetz MT (2006) In: Guisan JM (ed) Immobilization of enzymes and cells, Humana Press Inc., New Jersey.
10. Campàs M, Marty J-L (2006) In: Guisan JM (ed) Immobilization of enzymes and cells, Humana Press Inc., New Jersey
11. Yuce-Dursun B, Cigil AB, Dongez D, Kahraman MV, Ogan A, Demir S (2016) J Mol Catal B: Enzym 127:18–2510.1016/j.molcatb.2016.02.007 ↗
12. Preda G, Bizerea O, Vlad-Oros Be (2011) In: Serra PA (ed) Biosensors for health, environment and biosecurity, InTech, Rijeka.
13. Niederberger M, Pinna N (2009) Metal oxide nanoparticles in organic solvents: synthesis, formation, assembly and application. Springer Nature, Berlin10.1007/978-1-84882-671-7 ↗
14. Rao BG, Mukherjee D, Reddy BM (2017) In: Ficai D, Grumezescu A (eds) Nanostructures for Novel Therapy, Elsevier, Netherlands
15. Lind C, Gates SD, Pedoussaut NM, Baiz TI (2010) Materials 3:2567–258710.3390/ma3042567 ↗
16. Nam KH, Lee TH, Bae BS, Popall M (2006) J Sol-Gel Sci Technol 39:255–26010.1007/s10971-006-7884-y ↗
17. Nam S, Jang J, Kim K, Yun WM, Chung DS, Hwang J, Kwon OK, Chang T, Park CE (2011) J Mater Chem 21:775–78010.1039/C0JM00898B ↗
18. Eo Y, Lee TH, Kim SY, Kang JK, Han YS, Bae B (2005) J Polym Sci B Polym Phys 43:827–83610.1002/polb.20346 ↗
19. Çakmakçı E, Altıntaş Z, Kahraman MV, Kayaman-Apohan N (2015) J Vinyl Addit Technol 21:272–27710.1002/vnl.21398 ↗
20. Altıntaş Z, Çakmakçı E, Kahraman MV, Kayaman-Apohan N, Güngör A (2011) J Sol-Gel Sci Technol 58:612–61810.1007/s10971-011-2435-6 ↗
21. Bae J-Y, Yang S, Jin JH, Jung K, Kim J-S, Bae B-S (2011) J Sol-Gel Sci Technol 58:114–12010.1007/s10971-010-2363-x ↗
22. Morselli D, Bondioli F, Sangermano M, Messori M (2012) Polymer 53:283–29010.1016/j.polymer.2011.12.006 ↗
23. Kim J-S, Yang S, Park H, Bae B-S (2011) Chem Commun 47:6051–605310.1039/c1cc11297j ↗
24. Nguyen HH, Kim M (2017) Appl Sci Converg Technol 26:157–16310.5757/ASCT.2017.26.6.157 ↗
25. Oh JH, Kwak SY, Yang SC, Bae BS (2010) ACS Appl Mater Interfaces 2:913–91810.1021/am9008677 ↗
26. Jana S, Lim MA, Baek IC, Kim CH, Seok SI (2008) Mater Chem Phys 112:1008–101410.1016/j.matchemphys.2008.06.070 ↗
27. Kimmins SD, Wyman P, Cameron (2014) Polymer 55:416–42510.1016/j.polymer.2013.09.019 ↗
28. Cakmakci E, Danis O, Demir S, Mulazim Y, Kahraman MV (2013) J Microbiol Biotechnol 23:205–21010.4014/jmb.1209.09017 ↗
29. Bradford MM (1976) Anal Biochem 72:248–25410.1016/0003-2697(76)90527-3 ↗
30. Muhsir P, Çakmakçi E, Demir S, Ogan A (2018) Colloids Surf B 170:122–12810.1016/j.colsurfb.2018.05.062 ↗
31. Ellman GL, Courtney KD, Andres V, Featherstone RM (1961) Biochem Pharmacol 7:88–9510.1016/0006-2952(61)90145-9 ↗
32. Çakıroğlu B, Çiğil AB, Ogan A, Kahraman MV, Demir S (2018) Eng Life Sci 18:254–26210.1002/elsc.201700130 ↗
33. Abidi N, Hequet E, Tarimala S (2007) Text Res J 77:668–67410.1177/0040517507080621 ↗
34. Çakmakçi E, Muhsir P, Demir S (2017) Appl Biochem Biotechnol 18:1030–104710.1007/s12010-016-2266-6 ↗
35. Çakmakçi E, Yuce-Dursun B, Demir S (2017) React Funct Polym 111:38–4310.1016/j.reactfunctpolym.2016.11.006 ↗
36. Carioscia JA, Lu H, Stanbury JW, Bowman CN (2005) Dent Mater 21:1137–114310.1016/j.dental.2005.04.002 ↗
37. Nair DP, Cramer NB, Scott TF, Bowman CN, Shandas R (2010) Polymer 51:4383–438910.1016/j.polymer.2010.07.027 ↗
38. Mulazim Y, Cakmakci E, Kahraman MV (2013) Adv Polym Technol 32:416–42610.1002/adv.21289 ↗
39. Moradzadegan A, Ranaei‐Siadat S‐O, Ebrahim‐Habibi A, Barshan‐Tashnizi M, Jalili R, Torabi S‐F, Khajeh K (2010) Eng Life Sci 10:57–6410.1002/elsc.200900001 ↗
40. Yotova L, Medhat N (2012) Biotechnol Biotechnol Equip 26:3039–304310.5504/BBEQ.2012.0020 ↗
41. Stoilova O, Ignatova M, Manolova N, Godjevargova T, Mita DG, Rashkov I (2010) Eur Polym J 46:1966–197410.1016/j.eurpolymj.2010.08.005 ↗
42. Saleem M, Rafiq M, Seo S-Y, Lee KH (2016) Biosci Rep 36:1–910.1042/BSR20150154 ↗
43. Frasco MF, Fournier D, Carvalho F, Guilhermino L (2005) Biomarkers 10:360–37510.1080/13547500500264660 ↗