Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
권호 표지

Production of Thermostable $\alpha$-Amylase and Cellulase from Cellulomonas sp.

  • EMTIAZI, G., (Department of Biology, Faculty of Sciences, University of Isfahan) ;
  • I. NAHVI, (Department of Biology, Faculty of Sciences, University of Isfahan)
  • Published : 2004.12.01
Download PDF
⟨ Previous Next ⟩

Abstract

A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.

Keywords

References

  1. Bajpai, P. K. 1989. High-temperature alkaline $\alpha$-amylase from Bacillus licheniformis TCRDC-B13. Biotechnol. Bioeng. 33: 72-78 https://doi.org/10.1002/bit.260330110
  2. Bachina, E. M., L. G. Loginova, and M. V. Gernet. 1983. Selection of products of amylolytic enzymes among thermophilic microorganisms. Appl. Biochem. Microbiol. 18: 514-521
  3. Bradford, M. M. 1976. A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 144: 142- 146 https://doi.org/10.1016/0003-2697(85)90095-8
  4. Busch, J. E. and M. Stutzenbrger. 1997. Repression and inactivation of $\alpha$-amylase in Thermomonospora species during growth on cellobiase. J. Microbiol. 143: 2021-2026 https://doi.org/10.1099/00221287-143-6-2021
  5. Cowan, W. D. 1996. Animal feed, pp. 71-86. In: Goldfrey, T. and West, S. (eds.), Industrial Enzymology. Macmillan, London, U.K
  6. Emtiazi, G., I. Nahvi, and M. Salehbaig. 1992. Production of cellulase (exoglucanse) by fungi in different media. Research Bulletin of Isfahan University 10: 15-28
  7. Igarashi, K., Y. Hatada, H. Hagihara, K. Saeki, S. Takaiwa, T. Kobayashi, and S. Ito. 1998. Enzymatic properties of a novel liquefying amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences. Appl. Environ. Microbiol. 64: 3282-3289
  8. Johansson, T. and P. O. Nyman. 1993. Isoenzymes of lignin peroxidase and manganese peroxidase from the white-rot Basidiomycete. Arch. Biochem. Biophys. 300: 49-56
  9. Kim, K. U., G. Y. Gum, Jeong, B. S. Mung, and Y. C. Shin. 1995. Purification and characterization of $\alpha$-amylase from an alkaliphilic Bacillus strain GM 8901. Appl. Environ. Microbiol. 100: 106-108
  10. Mandel, M. and J. Weber. 1969. Exoglucanase activity by microorganisms. Adv. Chem. 95: 391-414
  11. Norman, B. E. 1979. The application of polysaccharide degrading enzymes in the starch industry, pp. 339-376. In: Berkeley RCW. Gooday GW, Eilwoo DC (eds.). Microbial Polysaccharides. Academic Press, London, U.K
  12. Okada, G. 1974. $\beta$-glucosidase activity in microorganisms. Biochem. J. 77: 33-42
  13. Vares, T., M. Kalsi, and A. Hatakka. 1995. Lignin peroxidases, manganese peroxidases, and other ligninolytic enzymes produced by Phlebia radiata during solid-state fermentation of wheat straw. Appl. Environ. Microbiol. 61: 3515-3520
  14. Yazdi, M. T., G. Wood Ward, and A. Radford. 1990. Cellulase production by Neurospora crassa: The enzymes of the complex and their regulation. Enzyme Microb. Technol. 12: 116-229