Abstract
Two chitinases, A and B, were purified from the culture supernatant of Streptomyces albovinaceus S-22 by ammonium sulphate fraction (80%) and Sephadex G-200 gel filtration. Both enzymes had molecular weights estimated to be 43 and 45 kDa by SDS polyacrylamide gel electrophoresis. The enzymes were active at 40 °C and pH 5.6 after 120 min, and stable at temperatures below 40 °C in the absence of chitin. The purified enzyme had potential for cell wall lysis of fungal pathogenesis tested.
References
Ames, G.F.L. 1974 Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Journal of Biological Chemistry 249, 634-644.
Jeuniaux, C. 1966 Chitinases. Methods in Enzymology 8, 644-651.
Mahadevan, B. & Crawford, D.L. 1997 Properties of the chitinase of the antifungal biocontrol agent Streptomyces lydicus WYEC 108. Enzyme and Microbial Technology 20, 489-493.
Mitsutomi, M., Hata, T. & Kuwahara, T. 1995 Purification and characterization of novel chitinases from Streptomyces griseus HUT 6037 Journal of Fermentation and Bioengineering 80, 153-158.
Monreal, J. & Reese, E.T. 1969 The chitinase of Serratia marcescens. Canadian Journal of Microbiology 15, 689-696.
Ohno, I., Armand, S., Hata, T., Nikaidou, N., Henrissat, B., Mitsutomi, M. & Watanabe, T. 1996 A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037. Journal of Bacteriology 178, 5065-5070.
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El-Sayed, ES., Ezzat, S., Ghaly, M. et al. Purification and characterization of two chitinases from Streptomyces albovinaceus S-22. World Journal of Microbiology and Biotechnology 16, 87–89 (2000). https://doi.org/10.1023/A:1008926214392
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DOI: https://doi.org/10.1023/A:1008926214392