화학공학소재연구정보센터
홈 로그인 로그아웃 연락처 사이트맵
Macromolecular Research, Vol.29, No.2, 120-128, February, 2021
DOI10.1007/s13233-021-9015-6  Export Citation
Electrostatic and Hydrogen Bond Immobilization of Trypsine onto pH-Sensitive N-Vinylpyrrolidone and 4-Vinylpyridine Radical co-Grafted Chitosan Based on Hydrogel
Shamo Zokhrab Tapdiqov1, 2, †
  • 1Department of Nanostructured Metal-polymer Catalysist, Institute Catalysis and Inorganic Chemistry, Azerbaijan National Academy of Sciences, H. Javid ave.113, AZ1143, Azerbaijan
  • 2Department of Prevention of Sand and Water Appearance, Oil and Gas Research and Design Institute, The State Oil Company of the Azerbaijan Republic, H.Zardabi ave.88a, Baku, AZ1012, Azerbaijan
E-mail:
The present investigation of new hydrogel based on chitosan was prepared by radical graft copolymerization of N-vinylpyrrolidone and 4-vinylpyridine with chitosan and cross-linking by N,N'-methylen-bis-acrylamide. The swelling behavior of the prepared hydrogel, with the optimal amount of gelator, was investigated. The hydrophilicity, and pH sensitivity of gel was suitable for trypsin carry. Trypsin was loaded onto the hydrogel enternal pores and surfaces by electrostatic interaction and hydrogen bond attachment. Several parameters, such as adsorbtion of pH value, loading time, and buffer solution concentration on trypsin loading amount, also enzyme activity were examined. According to the kinetic and FTIR, SEM spectroscopy analysis data trypsin was combination by the hydrogen bond and electrostatic interaction to the chitosan based structure. The hydrogen bonds were formed between -NH2, -CH2OH, >C=O, pyridine ring, -OH, and -NH- groups of carrier with -NH2, -COOH, -OH, >C=O, -NH-, disulfide bridge, ester groups of trypsine. In additional, at pH=5-8, the functional groups in the gel are partially ionized and take the form of -NH3 +, -OH2 +, >COH+. The protein is the same degree ionized in that medium, and the protein interacts electrostatically with the carrier.
Keywords:chitosan;graft copolymer;N-vinylpyrrolidone;4-vinylpyridine;hydrogel;immobilization;trypsin;hydrogen bond;electrostatic interaction;Michaelis constant
  1. Guedidi S, Yurekli Y, Deratani A, Dejardin P, Innocent C, Altinkaya SA, Roudesli S, Yemenicioglu A, J. Membr. Sci., 365(1-2), 59 (2010)
  2. Tapdiqov SZ, Azerbaijan Chem. J., 4, 129 (2010)
  3. Wahba MI, Hassan ME, Macromol. Res., 25(9), 913 (2017)
  4. Romdhane IB, Romdhane ZB, Gargouri A, Belghith H, J. Mol. Catal. B-Enzym., 68, 230 (2011)
  5. Abuchowski A, Van Es T, Palczuk NC, Davis FF, J. Biol. Chem., 252, 3578 (1977)
  6. Abuchowski A, McCoy JR, Palczuk NC, Van Es T, Davis FF, J. Biol. Chem., 252, 3582 (1977)
  7. Veronese FM, Biomaterials, 22, 405 (2001)
  8. Wang YS, Youngster S, Grace M, Bausch J, Bordens R, Wyss DF, Adv. Drug Deliv. Rev., 54, 547 (2002)
  9. Verma ML, Kumar SDA, Randhawa JS, Environ. Chem. Lett., 18, 315 (2020)
  10. Dincer A, Becerik S, Aydemir T, Int. J. Biol. Macromol., 50, 815 (2012)
  11. Mohamed SA, Aly AS, Mohamed TM, Salah HA, Appl. Biochem. Biotechnol., 144(2), 169 (2008)
  12. Orrego CE, Salgado N, Valencia JS, Giraldo GI, Giraldo OH, Cardona CA, Carbohydr. Polym., 79, 9 (2010)
  13. Metin AU, Macromol. Res., 21(10), 1145 (2013)
  14. Krajewska B, Enzyme Microb. Technol., 35(2-3), 126 (2004)
  15. Tapdiqov SZ, Zeynalov NA, Ahmedov ID, Melnikova NY, Nurullaev HH, Azerbaijan Chem. J., 2, 39 (2009)
  16. Hildonen S, Halvorsen TG, Reubsaet L, Proteomics, 14, 2031 (2014)
  17. Tapdiqov SZ, Zeynalov NA, Taghiyev DV, Humbatova SF, Mammedova SM, Nasiyyati EF, Babayeva DT, J. Chem. Soc. Pakistan., 37, 1112 (2015)
  18. Wu R, He B, Zhao G, Qian L, Li X, Carbohydr. Polym., 97, 523 (2013)
  19. Datta S, Christena LR, Rajaram YRS, 3 Biotech, 3, 1 (2013).
  20. Zelenetskii AN, Akopova TA, Kildeeva NR, Vikhoreva GA, Obolonkova ES, Zharov AA, Russian Chem. Bull., 52, 2073 (2003)
  21. Monzo A, Sperling E, Guttman A, Trac Trends in Anal. L Chem., 28, 854 (2009)
  22. Peterson DS, Rohr T, Svec F, Frechet JM, J. Anal. Chem., 74, 4081 (2002)
  23. Chanphai P, Tajmir-Riahi HA, J. Colloid Interface Sci., 461, 419 (2016)
  24. Nguyen HH, Kim M, Appl. Sci. Converg. Technol., 26, 157 (2017)
  25. Mohamad NR, Marzuki NHC, Buang NA, Huyop F, Wahab RA, Biotechnol. Biotechnol. Equip., 29, 205 (2015)
  26. Cristovao RO, Silverio SC, Tavares APM, Brigida AIS, Loureiro JM, Boaventura RAR, Macedo EA, Coelho MAZ, World J. Microbiol. Biotechnol., 28, 2827 (2012)
  27. Shin YH, Lo SH, Yang NS, Singco B, Cheng YJ, Wu CY, Chang IH, Huang HY, Lin CH, ChemPlusChem, 77, 982 (2012)
  28. Yamaguchi H, Miyazaki M, Proteomics, 13, 457 (2013)
  29. Silva TR, Rodrigues DP, Rocha JMS, Gil MH, Pinto SCS, Lopes-da-Silva JA, Guiomar AJ, Biochem. Eng. J., 104, 48 (2015)
  30. Goradia D, Cooney J, Hodnett B, Magner E, J. Mol. Catal. B-Enzym., 32, 231 (2005)
  31. Tapdiqov SZ, Zeynalov NA, Ahmedov ID, Nurullaev QQ, Mamedova SQ, Chem. Prob., 3, 406 (2010)
  32. Tapdigov SZ, Zeynalov NA, Tagiyev DB, Safaraliyeva SF, Gasimov EM, Hasanova MK, Nuraliyev AF, Sultanov CA, Chem. Prob., 16, 505 (2018)
  33. Tapdiqov SZ, Zeynalov NA, Humbatova SF, Nagiev JA, Isazadeh A, Hasanova M, Safaraliyeva S, Asian J. Chem., 28, 189 (2015)
  34. George W, Takenaka YS, Biochim. Biophys. Acta, 16, 570 (1955)
  35. El-Aassar MR, Al-Deyab SS, Kenawy ER, J. Appl. Polym. Sci., 127(3), 1873 (2013)
  36. Tapdiqov SZ, Cell. Chem. Technol., 54, 429 (2020)
  37. Rogovina SZ, Akopova TA, Vikhoreva GA, Gorbacheva IN, Zharov AA, Zelenetskii AN, Vysokomolekulyar. Soedinen., 42, 10 (2000)
  38. Gravitis YA, Bogdanov AY, Kokorevich AG, Zharov AA, Teeyaer RE, Zhulin VM, Lippmaa ET, Dokl. Akad. Nauk SSSR, 299, 1413 (1988)
  39. Reshmi R, Sanjay G, Sugunan S, Catal. Commun., 8, 393 (2007)
  40. Ganachaud C, Bernin D, Isaksson D, Holmberg K, Appl. Microbiol. Biotechnol., 979, 4403 (2013)
  41. Li D, Teoh WY, Gooding JJ, Selomulya C, Amal R, Adv. Funct. Mater., 20(11), 1767 (2010)
  42. Peng G, Zhao CX, Liu BL, Ye F, Jiang HW, Appl. Surf. Sci., 258(15), 5543 (2012)
  43. Chen H, Liu LH, Wang LS, Ching CB, Yu HW, Yang YY, Adv. Funct. Mater., 18(1), 95 (2008)
  44. Long J, Yu X, Xu E, Wu Z, Xu X, Jin Z, Jiao A, Carbohydr. Polym., 131, 98 (2015)
  45. Nakajima H, Kikuchi O, J. Mol. Struct., 365, 39 (1996)
  46. Shukla SK, Mishra AK, Arotiba OA, Mamba BB, Int. J. Biol. Macromol., 59, 46 (2013)
  47. Shirashi S, Imai T, Otagiri M, J. Control. Release, 25, 217 (1993)
  48. Secundo F, Chem. Soc. Rev., 42, 6250 (2013)
  49. Li S, Wu Z, Lu M, Wang Z, Li Z, Molecules, 18, 1138 (2013)
  50. Bronich TK, Vinogradov SV, Kabanov AV, Nano Lett., 1, 535 (2001)
  51. Kim HS, Kim JT, Jung YJ, Ryu SC, Son HJ, Kim YG, Macromol. Res., 15(1), 65 (2007)
  52. Nikolic T, Kostic M, Praskalo J, Pejic B, Petronijevic Z, Skundric P, Carbohydr. Polym., 82, 976 (2010)
  53. Rehman HU, Aman A, Silipo A, Qader SAU, Molinaro A, Ansari A, Food Chem., 139, 1081 (2013)
  54. Pluta J, Karolewicz B, Polim. Med., 34, 63 (2004)
  55. Wang J, Wang L, Yu H, Zain-ul-Abdin, Chen Y, Chen Q, Zhou W, Zhang H, Chen X, Int. J. Biol. Macromol., 88, 333 (2016)
  56. Zhou J, Lin Y, Ye L, Wang L, Zhou L, Hu H, Zhang Q, Yang H, Luo Z, Macromol. Res., 27(11), 1144 (2019)
  57. Kamburov M, Lalov I, Biotechnol. Biotechnol. Equip., 26, 156 (2012)