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Regulatory mutations affecting the synthesis of cellulase in Bacillus pumilus

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Abstract

A wild strain of Bacillus pumilus was investigated for cellulase production, and putative mutants of this strain were screened for catabolite repression insensitivity after chemical mutagenesis using ethyl methanesulphonate (EMS) as a mutagenic agent. Out of four classes of mutants studied and classified according to their cellulase induction rate and level of cellulase production in the presence of high concentrations of glucose (2.6%[w/v]), classes III and IV exhibited cellulase production up to 6.2 mg cellulase and 11.4 mg cellulase per gram of dry cell mass respectively. These mutants were referred to as catabolite repression-insensitive when compared to the wild strain which exhibited a total repression of cellulase synthesis under the same conditions. How EMS triggered the catabolite repression insensitivity in these mutants was not established. However this mutation brought out new strains of cellulase hyperproducers (mutants 6 and 11) in the presence of glucose when compared to other cellulase producers such as Aspergillus terreus, A. nidulans and Trichoderma reesei, which exhibited catabolite repression of cellulase synthesis. These mutants were selected as the most promising candidates for cellulase synthesis even at high glucose concentration.

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References

  • Ali, S. & Sayed, A. 1992 Regulation of cellulase biosynthesis in Aspergillus terreus. World Journal of Microbiology and Biotechnology 8, 73–75.

    Google Scholar 

  • Bagga, P.S., Sandhu, D.K. & Sharma, S. 1989 Catabolite repression of cellulase production in Aspergillus nidulans. Process Biochemistry 41, 41–45.

    Google Scholar 

  • DeCrombrugghe, B., Busby, S. & Buc, H. 1984 Cyclic AMP receptor protein: role in transcription activation. Science 224, 831–838.

    Google Scholar 

  • Hrmova, M., Petrakova, E. & Biely P. 1991 Induction of cellulose-and xylan-degrading enzyme systems in Aspergillus terreus by homo-and heterodisaccharides composed of glucose and xylose. Journal of General Microbiology 137, 541–547.

    Google Scholar 

  • Kawamori, M., Orikawa, Y., Takayama, K. & Takasawa, S. 1985 Preparation of mutants resistant to catabolite repression of Trichoderma reesei. Agricultural and Biological Chemistry 49, 2875–2879.

    Google Scholar 

  • Omafuvbe, B. 1998 Microbiological and biochemical changes during the fermentation of soyabeans for 'soydadawa'. PhD thesis, Microbiology Department, Obafemi Awolowo University, Ile-Ife, Nigeria.

    Google Scholar 

  • Pilz, I., Schwarz, E., Kilburn, D.G., Miller, R.C. Jr., Warren, R.A.J. & Gilkes, N.R. 1990 The tertiary structure of a bacterial cellulase determined by small angle X-ray scattering analysis. Biochemical Journal 271, 277–280.

    Google Scholar 

  • Shonukan, O.O. & Nwanfor, O.E. 1989 Isolation and partial characterization of temperature sensitive mutants of Bacillus subtilis. Microbios Letters 42, 43–46.

    Google Scholar 

  • Solomon, B.O., Amigun, B., Betiku, E., Ojumu, T.V. & Layokun, S.K. 1997 Optimization of cellulase production by Aspergillus flavus Linn isolate NSPR101 grown on bagasse. Journal of Nigerian Society of Chemical Engineers 16, 61–68.

    Google Scholar 

  • Somogyi, N. 1944 A photometric adaptation of the Somogyi method for the determination of glucose. Journal of Biological Chemistry 153, 375–380.

    Google Scholar 

  • Suzuki, H. & Kaneko, T. 1976 Degradation of barley glucan and lichenan by a Bacillus pumilus enzyme. Agricultural and Biological Chemistry 40, 577–586.

    Google Scholar 

  • Teather, R.M. & Wood, P.J. 1982 Use of congo-red-polysaccharide interaction in enumeration and characterization of cellulolytic bacteria from the Bovine rumen. Applied and Environmental Microbiology 43, 777–780.

    Google Scholar 

  • Teeri, T., Lehtovaara, P., Kaupinen, S., Salavuori, I. & Knowles, J. 1987 Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II. Gene 51, 43–52.

    Google Scholar 

  • Woodward, J., Affholter, K.A., Noles, K.K., Troy, N.T. & Gaslightwala, S.F. 1992 Does cellobiohydrolase II core protein from Trichoderma reesei disperse cellulose micro.brils? Enzyme and Microbial Technology 14, 625–630.

    Google Scholar 

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Kotchoni, S.O., Shonukan, O.O. Regulatory mutations affecting the synthesis of cellulase in Bacillus pumilus . World Journal of Microbiology and Biotechnology 18, 487–491 (2002). https://doi.org/10.1023/A:1015571022652

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  • DOI: https://doi.org/10.1023/A:1015571022652

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