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Effect of chitin sources on production of chitinase and chitosanase byStreptomyces griseus HUT 6037

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Abstract

The advantage of usingStreptomyces griseus HUT 6037 in the production of chitinase or chitosanase is that the organism is capable of hydrolyzing amorphous or crystal-line chitin and chitosan according to the type of the substrate used. We investigated the effects of the enzyme induction time and chitin sources, CM-chitosan and deacetylated chitosan (degree of deacetylation 75–99%), on production of chitosanase. We found that this strain accumulated chitosanase when cells were grown in the culture medium containing chitosanaceous substrates instead of chitinaceous substrates. The highest chitosanase activity was obtained at 4 days of cultivation with 99% deacetylated chitosan. Soluble chitosan (53% deacetylated chitosan) was found to induce chitinase as well as chitosanase. The specific activities of chitinase and chitosanase were 0.91 and 1.33 U/mg protein at 3 and 5 days, respectively. From the study of the enzymatic digestibility of various degrees of deacetylated chitosan, it was found that (GlcN)3, (GlcN)4 and (GlcN)5 were produced during the enzymatic hydrolysis reaction. The results of this study suggested that the sugar composition of (GlcN)3 was homogeneous and those of (GlcN)4 and (GlcN)5 were heterogeneous.

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References

  1. Kazuo, S. (1989) Development of chitin chitosan oligosaccharides.New Food Ind. 31: 17–25.

    Google Scholar 

  2. Koga, D. (1990) Chitinolytic enzymes.Sen-I Gakkaishi, 46: 581–585.

    Google Scholar 

  3. Takiguchi, Y. and K. Shimahara (1989) Productions and uses of N-acetylchitooligosaccharides and chitooligosaccharides by microorganism.Bio Industry 6: 616–621.

    CAS  Google Scholar 

  4. Joshi, S., M. Kozlowski, S. Richens, and D. M. Comberbach (1989) Chitinase and chitobiase production during fermentation of genetically improvedSerratia liquefaciens.Enzyme Microb. Technol. 11: 289–296.

    Article  CAS  Google Scholar 

  5. Mitsutomi, M., A. Ohtakara, T. Fukamizo, and S. Goto (1990) Action pattern ofAcromonas hydrophila chitinase on partiallyN-acetylated chitosan.Agric. Biol. Chem. 54: 871–877.

    CAS  Google Scholar 

  6. Mitsutomi, M., H. Kidoh, H. Tomita, and T. Watanabe (1995) The action ofBacillus circulans WL-12 chitinase on partiallyN-acetylated chitosan.Biosci. Biotech. Biochem. 59: 529–531.

    Article  CAS  Google Scholar 

  7. Mitsutomi, M., T. Hata, and T. Kuwahara (1995) Furification and characterization of novel chitinases fromStreptomyces griseus HUT 6037.J. Ferment Bioeng. 80: 153–158.

    Article  CAS  Google Scholar 

  8. Ohno, T., S. Armand, T. Hata, N. Nikaidou, B. Henrissar, M. Mitsutomi, and T. Watanabe (1996) A modular family 19 chitinase found in the prokaryotic organismStreptomyces griseus HUT 6037.J. Bacteriol. 178: 5065–5070.

    CAS  Google Scholar 

  9. Monreal, J. and E. T. Reese (1969) The chitinase ofSerratia marcescens.Can. J. Microbiol. 15: 689.

    Article  CAS  Google Scholar 

  10. Reid, J. D. and D. M. Ogrydziak (1981) Chitinase-over-producing mutant ofSerratia marcescens.Appl. Environ. Microbiol. 41: 664–669.

    CAS  Google Scholar 

  11. Roberts, R. L. and E. Cabib (1982)Serratia marcescens chitinase: one-step purification and use for the determination of chitin.Anal. Biochem. 127: 402–412.

    Article  CAS  Google Scholar 

  12. Fuchs, R. L., S. A. McPherson, and D. J. Drahos (1986) Cloning of aSerratia marcescens gene encoding chitinase.Appl. Environ. Microbiol. 51: 504–509.

    CAS  Google Scholar 

  13. Ulhoa, C. J. and J. F. Peberdy (1992) Purification and some properties of the extracellular chitinase produced byTrichoderma harzianum.Enzyme Microb. Technol. 14: 236–240.

    Article  CAS  Google Scholar 

  14. Neugebauer, E., B. Gamache, and R. Brzezinski (1991) Chitinolytic properties ofStreptomyces lividans.Arch. Mircobiol. 156: 192–197.

    CAS  Google Scholar 

  15. Robbins, P. W., C. Albright, and B. Benfield (1983) Cloning and expression of aStreptomyces plicatus chitinase (chitinase-63) inEscherichia coli.J. Biol. Chem. 263: 443–447.

    Google Scholar 

  16. Vyas, P. and M. V. Deshpande, (1989) Chitinase production byMyrothecium verrucaria and its significance for fungal mycelia degradation.J. Gen. Appl. Microbiol. 35: 343–350.

    Article  CAS  Google Scholar 

  17. Zikakis, J. P. (1984)Chitin, Chitosan, and Related Enzymes. pp. 161–179. Academic Press, Orlando, USA.

    Google Scholar 

  18. Muzzarelli, R. A. A. (1977)Chitin. pp. 164–167. Pergamon Press, Oxford, UK.

    Google Scholar 

  19. Ohtakara, A., H. Ogata, Y. Taketomi, and M. Mitsutomi (1984) Purification and characterization of chitosanase fromStreptomyces griseus pp. 147–160, Academic Press, Orlando, USA.

    Google Scholar 

  20. Kim, K., C. W. Lee, E. Y. Lee, and S. M. Chang (1996) Optimal production ofN-acetyl-β-D-glucosamine using chitinolytic enzyme.Kor. J. Biotechnol. Bioene 11: 696–703.

    Google Scholar 

  21. Berger, L. R. and D. M. Reynolds (1958) The chitinase system of a strain ofStreptomyces griseus.Biochim. Biophys. Acta 29: 522–534.

    Article  CAS  Google Scholar 

  22. Mima, S., M. Miya, R. Iwamoto, and S. Yoshikawa (1988) Highly deacetylation chitosan and its properties.Appl. Polymer Sci. 28: 1909–1917.

    Article  Google Scholar 

  23. Sannan, T., K. Kurita, and Y. Iwakura (1976) Effect of deacetylation on solubility.Makromol. Chem. 177: 3589–3600.

    Article  CAS  Google Scholar 

  24. Domszy, J. G. and G. A. F. Roberts (1985) Evaluation of infrared spectroscopic techniques for analyzing chitosan.Makromol. Chem. 186: 1671–1677.

    Article  CAS  Google Scholar 

  25. Sannan, T., K. Kurita, K. Ogura and Y. Iwakura (1978) Studies on chitin: 7. I. R. spectroscopic determination of degree of deacetylation.Polymer 19: 458–459.

    Article  CAS  Google Scholar 

  26. Tokura, S., N. Nishi, and A. Tsutsumi (1983) Studies on chitin 8. some properties of water soluble chitin derivatives.Polymer 15: 485.

    Article  CAS  Google Scholar 

  27. Ohtakara, A. (1988) Chitosanase fromStreptomyces griseus.Method Enzymol. 161: 64–69.

    Google Scholar 

  28. Rondle, G. J. M. and W. T. J. Morgan (1955) The determination of glucosamine and galactosamin.J. Biochem. 61: 586–589.

    CAS  Google Scholar 

  29. Reissig, J. L., J. L. Strominger and L. F. Leloir (1955) A modified colorimetric method for the estimation ofN-acetylamino sugars.J. Biol. Chem. 27: 959–966.

    Google Scholar 

  30. Imoto, T. and K. Yagishita (1971) A simple activity measurement of lysozyme.Agric. Biol. Chem. 35: 1154–1156.

    CAS  Google Scholar 

  31. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Anal. Biochem. 72: 248–254.

    Article  CAS  Google Scholar 

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Correspondence to Kwang Kim.

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Kim, K., Ji, HS. Effect of chitin sources on production of chitinase and chitosanase byStreptomyces griseus HUT 6037. Biotechnol. Bioprocess Eng. 6, 18–24 (2001). https://doi.org/10.1007/BF02942245

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  • DOI: https://doi.org/10.1007/BF02942245

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