Browse > Article
http://dx.doi.org/10.5012/bkcs.2012.33.7.2181

Covalent Immobilization of Trypsin on a Novel Aldehyde-Terminated PAMAM Dendrimer  

Hamidi, Aliasghar (Drug Applied Research Center, Tabriz University of Medical Sciences)
Rashidi, Mohammad R. (Drug Applied Research Center, Tabriz University of Medical Sciences)
Asgari, Davoud (Drug Applied Research Center, Tabriz University of Medical Sciences)
Aghanejad, Ayuob (Department of Nuclear Pharmacy, Faculty of Pharmacy, Tehran University of Medical Sciences)
Davaran, Soodabeh (Drug Applied Research Center, Tabriz University of Medical Sciences)
Publication Information
Bulletin of the Korean Chemical Society / v.33, no.7, 2012 , pp. 2181-2186 More about this Journal
Abstract
Dendrimers are a novel class of nonlinear polymers and due to their extensive applications in different fields, called versatile polymers. Polyamidoamine (PAMAM) dendrimers are one of the most important dendrimers that have many applications in nanobiotechnology and industry. Generally aldehyde terminated dendrimers are prepared by activation of amine terminated dendrimers by glutaraldehyde which has two problems, toxicity and possibility of crosslink formation. In this study, novel aldehyde-terminated PAMAM dendrimer was prepared and used for covalent immobilization of trypsin by the aim of finding a special reagent which can prevent crosslinking and deactivation of the enzyme. For this purpose aminoacetaldehydedimethylacetal (AADA) was used as spacer group between aldehyde-terminated PAMAM and trypsin.The findings of this study showed that immobilization of trypsin not only resulted higher optimal temperature, but also increased the thermal stability of the immobilized enzyme in comparison to the free enzyme.
Keywords
Immobilization; Trypsin; Synthesis; PAMAM dendrimer; Aldehyde terminated dendrimers;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
Times Cited By Web Of Science : 0  (Related Records In Web of Science)
연도 인용수 순위
1 de Miguel Bouzas, T.; Barros-Velazquez, J.; Gonzalez Villa, T. Protein and Peptide Letters 2006, 13, 645.   DOI
2 Amini, K. A. K.; Mohammad-Hossein Sorouraddin, M. H. S.; Mohammad-Reza Rashidi, M. R. R. Canadian Journal of Chemistry 2010, 89, 1.
3 Dutta, T.; Jain, N. K.; McMillan, N. A. J.; Parekh, H. S. Nanomedicine: Nanotechnology, Biology and Medicine 2010, 6, 25.
4 Lopez, J.; Imperial, S.; Valderrama, R.; Navarro, S. Clinica Chimica Acta 1993, 220, 91.   DOI
5 Chang, M.-Y.; Juang, R.-S. Enzyme and Microbial Technology 2005, 36, 75.   DOI
6 Akkus Cetinus, S.; Nursevin Oztop, H. Enzyme and Microbial Technology 2003, 32, 889.   DOI
7 Chellapandian, M. Process Biochemistry 1998, 33, 169.   DOI
8 Gupta, U.; Agashe, H. B.; Asthana, A.; Jain, N. K. Nanomedicine: Nanotechnology, Biology and Medicine 2006, 2, 66.   DOI
9 Demanuele, A.; Attwood, D. Advanced Drug Delivery Reviews 2005, 57, 2147.   DOI
10 Yang, W.; Cheng, Y.; Xu, T.; Wang, X.; Wen, L.-P. European Journal of Medicinal Chemistry 2009, 44, 862.   DOI
11 Uehara, T.; Ishii, D.; Uemura, T.; Suzuki, H.; Kanei, T.; Takagi, K. et al. Bioconjugate Chemistry 2010, 21, 175.   DOI
12 Kurtoglu, Y. E.; Mishra, M. K.; Kannan, S.; Kannan, R. M. International Journal of Pharmaceutics 2010, 384, 189.   DOI
13 Lutz, J.-F.; Borner, H. G. Progress in Polymer Science 2008, 33, 1.   DOI   ScienceOn
14 Hamerska-Dudra, A.; Bryjak, J.; Trochimczuk, A. W. Enzyme and Microbial Technology 2007, 41, 197.   DOI
15 Blanco, R. M.; Calvete, J. J.; Guisan, J. M. Enzyme and Microbial Technology 1989, 11, 353.   DOI
16 Fernandez-Lafuente, R.; Rodriguez, V.; Mateo, C.; Penzol, G.; Hernandez-Justiz, O.; Irazoqui, G. et al. Journal of Molecular Catalysis - B Enzymatic 1999, 7, 181.   DOI
17 Fréchet, J. M. J.; Tomalia, D. A. Laboratory Synthesis of Poly(amidoamine) (PAMAM) Dendrimers Dendrimers and Other Dendritic Polymers; 2001; p 587.
18 Ibrahim, K. S. Journal of Microbiology and Biotechnology 2011, 21, 20.   DOI
19 Wati, M. R.; Thanabalu, T.; Porter, A. G. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1997, 1352, 56.   DOI
20 Nouaimi, M.; Moschel, K.; Bisswanger, H. Enzyme and Microbial Technology 2001, 29, 567.   DOI
21 Mhaske, S.; Kadam, P. G.; Matunga, M. International Journal of Applied Engineering Research; Dindigul 2010.
22 Klajnert, B.; Bryszewska, M. Acta Biochimica Polonica. 2001, 48, 199.
23 Gaertner, H. F.; Cerini, F.; Kamath, A.; Rochat, A.-F.; Siegrist, CA.; Menin, L. et al. Bioconjugate Chemistry 2011, 22, 1103.   DOI
24 Tao, L.; Geng, J.; Chen, G.; Xu, Y.; Ladmiral, V.; Mantovani, G. et al. Chemical Communications 2007, 3441.
25 Nanjwade, B. K.; Bechra, H. M.; Derkar, G. K.; Manvi, F. V.; Nanjwade, V. K. European Journal of Pharmaceutical Sciences 2009, 38, 185.   DOI
26 Gillies, E.; Frechet, J. Drug Discovery Today 2005, 10, 35.   DOI
27 Endo, K.; Ito, Y.; Higashihara, T.; Ueda, M. European Polymer Journal 2009, 45, 1994.   DOI
28 Cheng, Y.; Li, M.; Xu, T. European Journal of Medicinal Chemistry 2008, 43, 1791.   DOI
29 Cheng, Y.; Qu, H.; Ma, M.; Xu, Z.; Xu, P.; Fang, Y. et al. European Journal of Medicinal Chemistry 2007, 42, 1032.   DOI
30 Biricova, V.; Laznickova, A. Bioorganic Chemistry 2009, 37, 185.   DOI
31 Cloninger, M. J. Current Opinion in Chemical Biology 2002, 6, 742.   DOI   ScienceOn
32 Ma, M.; Cheng, Y.; Xu, Z.; Xu, P.; Qu, H.; Fang, Y. et al. European Journal of Medicinal Chemistry 2007, 42, 93.   DOI