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  • 1
    Electronic Resource
    Electronic Resource
    Growth of Cellulomonas sp. ATCC 21399 on different polysaccharides as sole carbon source Induction of extracellular enzymes (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 480-484 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Growth and extracellular enzyme production of Cellulomonas sp. ATCC 21399 on carboxymethylcellulose (CMC), microcrystalline cellulose (Avicel), xylan, galactomannan and starch were compared. The bacteria grew poorly on CMC, whereas high cell densities were obtained on the other substrates. Growth on Avicel resulted in extracellular enzyme activities against CMC, Avicel, xylan, galactomannan and amylose. By contrast, growth on xylan, galactomannan and starch induced only the enzymes neccessary for the degradation of the growth substrate. Extracellular proteinase activity could be measured during growth on all substrates but CMC, and the possibility of proteolytic inactivation of some of the unstable enzymes (i.e. Avicelase and amylase) in discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269072
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  • 2
    Electronic Resource
    Electronic Resource
    Growth and enzyme production of Cellulomonas sp. ATCC 21399 on microcrystalline cellulose. Effects of increasing concentration of a mineral medium (1989)
    Springer
    Applied microbiology and biotechnology 30 (1989), S. 535-539 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The kinetics and production of different extracellular enzyme activities were studied during growth of Cellulomonas sp. ATCC 21399 on 2% Avicel with different concentrations of M9 mineral medium. The lag phase and the doubling time increased with increasing ionic strength of the medium. The highest cell density was obtained during growth at 5 x M9 mineral medium and Cellulomonas grew well at this high salinity. The enzyme activities against carboxymethylcellulose and xylan increased with increasing concentration of M9 medium up to 5 x M9. By contrast, activities against microcrystalline cellulose (Avicel), galactomannan and amylose decreased with increasing concentration of M9 medium. The extracellular proteinase activity increased with increasing concentration of M9 medium, and it is possible that the lability of the cellulolytic and amylolytic enzymes may be due to their susceptibility to proteolytic inactivation by the extracellular proteinases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00263861
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  • 3
    Electronic Resource
    Electronic Resource
    Electrophoretic and enzymatic studies on the crude extracellular enzyme system of the cellulolytic bacterium Cellulomonas sp. ATCC 21399 (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 59-64 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cellulomonas sp. ATCC 21399 produced extracellular enzyme activities against Avicel, H3PO4-swollen Avicel, carboxymethylcellulose, (1-3, 1-4)-β-D-heteroglucan, xylan, galactomannan, and amylose drying growth on microcrystalline cellulose. No extracellular cellobiase activity was produced. Crossed immunoelectrophoresis of the crude extracellular enzyme system revealed 15 immunologically distinct immunoprecipitates. The immunoprecipitates of endoglucanase A, endoglucanase B and the xylanase appeared heterogeneous with several optima, whereas the immunoprecipitates of endoglucanase C and the amylase appeared homogeneous. The heterogeneity of endoglucanase A, endoglucanase B and xylanase was also visualized using electrofocusing-immunoelectrophoresis. Electro-focusing could resolve the activity against carboxymethylcellulose into six peaks, whereas only one peak of activity against Avicel was observed. The later peak coincided with the major peak of activity against carboxymethylcellulose with isoelectric point between pH 4.0-5.0.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260340108
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  • 4
    Electronic Resource
    Electronic Resource
    Degradation of microcrystalline cellulose: Synergism between different endoglucanases of Cellulomonas sp. ATCC 21399 (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 121-123 
    Details
    ISSN: 0006-3592
    Keywords: Cellulomonas sp. ; Trichoderma reesei ; short fiber formation ; Avicel ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Three immunologically and enzymatically distinct endoglucanases of Cellulomonas sp. ATCC 21399 were purified previously. Endoglucanase A and endoglucanase B acted synergistically on microcrystalline cellulose (Avicel), whereas no synergistic action was observed between endoglucanase B or endoglucanase C. Only endoglucanase A was capable of hydrolyzing Avicel when acting alone and this enzyme resulted in “short fiber formation” when acting on Avicel. The end product of hydrolysis of acid swollen Avicel produced by the three endoglucanases was in all cases dominated by cellobiose and showed lower content of glucose and cellotriose. Higher cellodextrins appeared as transient end products. The results indicate that the function of endoglucanase A in the cellulase system of Cellulomonas might be very similar to the function of the cellobiohydrolases of Trichoderma reesei.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260390118
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  • 5
    Electronic Resource
    Electronic Resource
    Purification of two immunologically distinct endoglucanases without affinity for microcrystalline cellulose from Cellulomonas sp. ATCC 21399 (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 65-71 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Two endoglucanases (endoglucanase B and endoglucanase C) without affinity for cellulose were purified from the culture broth of Cellulomonas sp. ATCC 21399 using gelfiltration and ion exchange chromatography. Fused rocket immunoelectrophoresis was used to select the fractions with the highest content of endoglucanase and lowest content of contaminating proteins. The endoglucanases were purified to immunological homogeneity. In addition both endoglucanases were homogeneous when analyzed by sodium dodecyl sulfate - polyacrylamide gel electrophoresis (molecular weights of endoglucanase B and endoglucanase C were 67000 and 25000, respectively). Endoglucanase B was homogeneous when studied by isoelectric focusing showing one protein band at pl 4.3. Both endoglucanases lacked activity against microcrystalline cellulose (Avicel) and showed similar endo action on carboxymethylcellulose (CMC). Endoglucanase B had a high specific activity against CMC, H3PO4-swollen Avicel and xylan, but showed no activity against galactomannan. In contrast, endoglucanase C showed activity against both CMC, xylan, and galactomannan all being polysaccharide substrates linked with β-1-4-D-glucoside bonds. The specific activity of endoglucanase C against H3PO4-swollen Avicel was low.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260340109
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  • 6
    Electronic Resource
    Electronic Resource
    A standard formula for the determination of the initial rate of hydrolysis of carboxymethylcellulose (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 409-414 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The integrated rate equation of Huang, originally used to describe the hydrolysis of insoluble acid treated cellulose, is shown equally applicable in describing the hydrolysis of carboxymethylcellulose (CMC) using a dilution series of Cellulomonas sp. ATCC 21399 crude cellulase as enzyme preparation. Interpretation of the progress curves of hydrolysis of CMC according to the integrated rate equation is used to calculate a standard formula for the conversion of the rate of hydrolysis into the initial velocity of hydrolysis. The validity of the standard formula is tested, using enzyme preparations from Cellulomonas grown under varied conditions, and enzyme preparations containing purified endoglucanases from Cellulomonas.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270404
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  • 7
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    Growth of Cellulomonas sp. ATCC 21399 on different polysaccharides as sole carbon source Induction of extracellular enzymes (1988)
    Springer
    Details
    Publication Date: 1988-11-01
    Print ISSN: 0175-7598
    Electronic ISSN: 1432-0614
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer
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