Abstract
The specific nature of the chitosanase activity of the strain Bacillus sp. 739 was determined. Maximum enzyme activity was observed in a medium containing biomass of the fruiting bodies of the fungus Macrolepiota procera. The chitosanase was purified to homogeneity by chromatography on DEAE-Sephadex A-50 and Toyopearl HW-50. The molecular weight of the enzyme assessed by electrophoresis (the Laemmli procedure) approximated 46 kDa. The temperature and pH optima of the purified chitosanase were in the ranges 45–55°C and 6.0–6.5, respectively. Time to half-maximum inactivation of the enzyme at 50°C was equal to 1 h. With colloidal chitosan as the substrate, the value of K М of the purified chitosanase was equal to 25 mg/ml. The enzyme also exhibited a weak ability to hydrolyze colloidal chitin.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
REFERENCES
Tiunova, N.A., Uspekhi biologicheskoi khimii, 1989, vol. 30, pp. 199–219.
Mitsutomi, M., Kidon, H., Tomita, H., and Watanabe, T., Biosci. Biotech. Biochem., 1995, vol. 59, no.3, pp. 529–531.
Park, J.K., Shimono, K., Ochiai, N., et al., J. Bacteriol., 1999, vol. 181, no.21, pp. 6642–6649.
Fukamizo, T., Ohkawa, T., Ikeda, Y., and Goto, S., Biochim. Biophys. Acta, 1994, vol. 1205, no.2, pp. 183–188.
Fenton, D.M. and Eveleigh, D.E., J. Gen. Microbiol., 1981, vol. 126, no.1, pp. 151–165.
Hedges, A. and Wolfe, R.S., J. Bacteriol., 1974, vol. 120, no.2, pp. 844–853.
Price, J.S. and Storck, R., J. Bacteriol., 1975, vol. 124, no.3, pp. 1574–1585.
Pelletier, A. and Sygusch, J., Appl. Environ. Microbiol., 1990, vol. 56, no.3, pp. 844–848.
Yamasaki, Y., Hayashi, I., Ohta, Y., et al., Biosci. Biotechnol. Biochem., 1993, vol. 57, no.3, pp. 444–449.
Pedraza-Reyes, M. and Gutierrez-Corona, F., Arch. Microbiol., 1997, vol. 168, no.4, pp. 321–327.
Mitsutomi, M., Isono, M., Uchiyama, A., et al., Biosci. Biotechnol. Biochem., 1998, vol. 62, no.11, pp. 107–114.
Grenier, J. and Asselin, A., Mol. Plant-Microbe Interact., 1990, vol. 3, no.6, pp. 401–407.
Osswald, W.F., Shapiro, J.P., Doostdar, H., et al., Plant Cell Physiol., 1994, vol. 35, no.5, pp. 811–820.
Japan Patent, 1990, no. 3277277.
Maksimov, V.I., Rodoman, V.E., and Luntsevich, V.G., Prikl. Biokhim. Mikrobiol., 1997, vol. 33, no.4, pp. 355–362.
Rhoades, J. and Roller, S., Appl. Environ. Microbiol., 1999, vol. 66, no.1, pp. 80–86.
Somashekar, D. and Joseph, R., Biores. Technol., 1996, vol. 55, no.1, pp. 35–45.
Melent'ev, A.I. and Aktuganov, G.E., Prikl. Biokhim. Mikrobiol., 1999, vol. 35, no.6, pp. 624–628.
Aktuganov, G.E., Melent'ev, A.I., and Usanov, N.G., Biotechnologiya, 2001, no. 3, pp. 25–33.
Il'ina, A.V., Varlamov, V.P., Melent'ev, A.I., and Aktuganov, G.E., Prikl. Biokhim. Mikrobiol., 2001, vol. 37, no.2, pp. 160–163.
Veselov, S.Yu., Ivanova, T.N., Simonyan, M.V., and Melent'ev, A.I., Prikl. Biokhim. Mikrobiol., 1998, vol. 34, no.2, pp. 175–179.
Feofilova, E.P., Tereshina, V.M., and Memorskaya, A.S., Mikrobiologiya, 1995, vol. 64, no.1, pp. 27–31.
Sinitsyn, A.P., Chernoglazov, V.M., and Gusakov, A.V., Metody izucheniya i svoistva tsellyuloliticheskikh fermentov (Methods of Study and Properties of Cellulose-Lytic Enzymes), Itogi Nauki Tekh., Ser.: Biotekhnologiya, Moscow: VINITI, 1993, vol. 25.
Aktuganov, G.E., Properties of Chitinase of Bacillus sp. 739, an Antagonist of Phytopathogenic Fungi, Cand. Sc. (Biol.) Dissertation, Ufa: In-t biologii UNTs RAN, 2000.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Aktuganov, G.E., Shirokov, A.V. & Melent'ev, A.I. Isolation and Characterization of Chitosanase from the Strain Bacillus sp. 739. Applied Biochemistry and Microbiology 39, 469–474 (2003). https://doi.org/10.1023/A:1025492518159
Issue Date:
DOI: https://doi.org/10.1023/A:1025492518159