Abstract
The activity of components of the extracellular cellulase system of the thermophilic fungus Sporotrichum thermophile showed appreciable differences between strains; β-glucosidase (EC 3.2.1.21) was the most variable component. Although its endoglucanase (EC 3.2.1.4) and exoglucanase (EC 3.2.1.91) activities were markedly lower, S. thermophile degraded cellulose faster than Trichoderma reesei. The production of β-glucosidase lagged behind that of endoglucanase and exoglucanase. The latter activities were produced during active growth. When growth was inhibited by cycloheximide treatment, the hydrolysis of cellulose was lower than in the control in spite of the presence of both endoglucanase and exoglucanase activities in the culture medium. Degradation of cellulose was a growth-associated process, with cellulase preparations hydrolyzing cellulose only to a limited extent. The growth rate and cell density of S. thermophile were similar in media containing cellulose or glucose. A distinctive feature of fungal development in media incorporating cellulose or lactose (inducers of cellulase activity) was the rapid differentiation of reproductive units and autolysis of hyphal cells to liberate propagules which were capable of renewing growth immediately.
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- Coutts A. D., Smith R. E. Factors influencing the production of cellulases by Sporotrichum thermophile. Appl Environ Microbiol. 1976 Jun;31(6):819–825. doi: 10.1128/aem.31.6.819-825.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hulme M. A., Stranks D. W. Regulation of cellulase production by Myrothecium verrucaria grown on non-cellulosic substrates. J Gen Microbiol. 1971 Dec;69(2):145–155. doi: 10.1099/00221287-69-2-145. [DOI] [PubMed] [Google Scholar]
- Jeffries T. W., Choi S., Kirk T. K. Nutritional Regulation of Lignin Degradation by Phanerochaete chrysosporium. Appl Environ Microbiol. 1981 Aug;42(2):290–296. doi: 10.1128/aem.42.2.290-296.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Mandels M. Microbial sources of cellulase. Biotechnol Bioeng Symp. 1975;(5):81–105. [PubMed] [Google Scholar]
- Ng T. K., Weimer T. K., Zeikus J. G. Cellulolytic and physiological properties of Clostridium thermocellum. Arch Microbiol. 1977 Jul 26;114(1):1–7. doi: 10.1007/BF00429622. [DOI] [PubMed] [Google Scholar]
- Ng T. K., Zeikus J. G. Comparison of Extracellular Cellulase Activities of Clostridium thermocellum LQRI and Trichoderma reesei QM9414. Appl Environ Microbiol. 1981 Aug;42(2):231–240. doi: 10.1128/aem.42.2.231-240.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Romanelli R. A., Houston C. W., Barnett S. M. Studies on thermophilic cellulolytic fungi. Appl Microbiol. 1975 Aug;30(2):276–281. doi: 10.1128/am.30.2.276-281.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SMOGYI M. Notes on sugar determination. J Biol Chem. 1952 Mar;195(1):19–23. [PubMed] [Google Scholar]
- Shoemaker S. P., Raymond J. C., Bruner R. Cellulases: diversity amongst improved Trichoderma strains. Basic Life Sci. 1981;18:89–109. doi: 10.1007/978-1-4684-3980-9_7. [DOI] [PubMed] [Google Scholar]
- Stutzenberger F. J. Cellulolytic activity of Thermomonospora curvata: optimal assay conditions, partial purification, and product of the cellulase. Appl Microbiol. 1972 Jul;24(1):83–90. doi: 10.1128/am.24.1.83-90.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Updegraff D. M. Semimicro determination of cellulose in biological materials. Anal Biochem. 1969 Dec;32(3):420–424. doi: 10.1016/s0003-2697(69)80009-6. [DOI] [PubMed] [Google Scholar]