Effect of the charge of the interface surface on the structure and activity of trypsin in reversed mycelles

Russian Journal of Bioorganic Chemistry - Tập 34 - Trang 359-363 - 2008
Yu. A. Valiullina1, E. A. Stupishina1, N. N. Vylegzhanina1, B. Z. Idiyatullin1, Yu. F. Zuev1
1Kazan Institute of Biochemistry and Biophysics, Kazan Scientific Center, Russian Academy of Sciences, Kazan, Russia

Tóm tắt

The effect of the sign and value of the charge of the interface surface on the catalytic activity of trypsin in systems of reversed mycelles was investigated. n-Butanol was used for the modification of the phase interface in dispersions of reversed mycelles based on anionic sodium bis(2-ethylhexyl)sulfosuccinate (AOT) and cationic cetyltrimethylammonium bromide (CTAB). A direct correlation between changes in the state of reversed mycelles and the structure of solubilized enzyme under the action of butanol was obtained. It was shown that the enzyme activity is determined by the quantity of butanol solubilized by the reversed mycelles.

Tài liệu tham khảo

Berezin, I.V., Action of Enzymes in Inverted Mycelles, 39 Bakh Readings, Moscow: Nauka, 1985. Matinek, K., Levashov, A.V., Klyachko, N.L., Khmelnitsky, Yu.L., and Berezin, I.V., Eur. J. Biochem., 1986, vol. 155, pp. 453–468. Chang, G.-G., Huang, T.-M., and Hung, H.-C., Proc. Natl. Sci. Counc. Repub. China B, 2000, vol. 24, pp. 89–100. Holmberg, K., in Handbook in Microemulsion Science and Technology, Kumar, P. and Mittal, K.L., Eds., New York: Marcel Dekker, 1999, pp. 713–742. Klyachko, N.L. and Levashov, A.V., Curr. Opp. Colloid Interface Sci., 2003, vol. 8, pp. 179–186. Creagh, A.L., Prausnits, J.M., and Blanch, H.W., Enzyme Microb. Technol., 1993, vol. 15, pp. 383–392. Martinek, K., Yatsimirsky, A.K., Levashov, A.V., and Beresin, I.V., in Micellization, Solubilization, and Microemulsions: The Kinetic Theory and the Mechanisms of Micellar Effects on Chemical Reactions, Mittal, K.L., Ed., New York: Plenum, 1977, pp. 489–505. Aguilar, L.F., Abuin, E., and Lissi, E., Arch. Biochem. Biophys., 2001, vol. 388, pp. 231–236. Das, D., Roy, S., Mitra, R.N., Dasgupta, A., and Das P.K., Chemistry, 2005, vol. 11, pp. 4881–4889. Almeida, F.C., Valente, A.P., and Chaimovich, H., Biotechnol. Bioeng., 1998, vol. 59, pp. 360–363. Stupishina, E.A., Faizullin, D.A., Zakhartchenko, N.L., Fedotov, V.D., and Zuev, Yu.F., Mendeleev Commun., 2001, pp. 237–240. Lang, J., Lalem, N., and Zana, R.J., Phys. Chem., 1991, vol. 95, pp. 9533–9544. Bisal, S., Bhattacharya, P.K., and Moulik, S.P., J. Phys. Chem., 1990, vol. 94, pp. 350–355. Wong, M., Thomas, J.K., and Nowak, T., J. Am. Chem. Soc., 1977, vol. 99, pp. 4730–4736. Lu, Zh., Karne, S., Kolodecik, T., and Gorelick, F.S., Am. J. Physiol. Gastrointest. Liver Physiol., 2002, vol. 282, pp. 501–507. Simon, L.M., Kotormán, M., Garab, G., and Laszkó, I., Biochem. Biophys. Res. Commun., 2001, vol. 280, pp. 1367–1371. Martinek, K., Levashov, A.V., and Berezin, I.V., Mol. Biol. (Moscow), 1970, vol. 4, pp. 517–527. Levashov, A.V., Klyachko, N.L., Pantin, V.I., Khmel’nitskii, Yu.L., and Martinek, K., Bioorg. Khim., 1980, vol. 6, pp. 929–942. Fandavis, N.W., Babu, R.L., and Deshpande, A., Biochimie, 1998, vol. 80, pp. 1025–1030. Belova, A.B., Mozhaev, V.V., Levashov, A.V., Sergeeva, M.V., Martinek, K., and Khmel’nitskii, Yu.A., Biokhimiya (Moscow), 1991, vol. 56, pp. 1923–1945. Klesov, A.A. and Berezin, I.V., Fermentativnyi kataliz (Enzymatic Catalysis), Moscow: Vysshaya Shkola, 1980. Goronovskii, I.T., Nazarenko, Yu.P., and Nekryach, E.F., Kratkii spravochnik po khimii (Concise Handbook on Chemistry), Kiev: Akad. nauk Ukr. SSR, 1963. Zuev, Yu.F., Mirgorodskaya, A.B., and Idiyatullin, B.Z., Appl. Magn. Res., 2004, vol. 27, pp. 489–500. Reshetnyak, Ya.K. and Burshtein, E.A., Biofizika, 1997, vol. 42, pp. 785–795. Bresler, S.E., Shampan’, M., and Frenkel’, S.Ya., Biokhimiya (Moscow), 1961, vol. 26, pp. 909–915. Zuev, Yu.F., Vylegzhanina, N.N., and Zakhartchenko, N.L., Appl. Magn. Reson., 2003, vol. 25, pp. 29–42.