Synergism of cellulases from Trichoderma reesei in the degradation of cellulose

Henrissat, B; Driguez, H; Viet, C; Schuelein, M

doi:10.1038/nbt0885-722

Title: Synergism of cellulases from Trichoderma reesei in the degradation of cellulose

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Abstract

The action of cellobiohydrolases I and II (CBHI and CBHII) and endoglucanases I and II (EGI and EGII) purified from Trichoderma reesei was evaluated against various substrates. CBHI degraded the ..beta..-D-glucan from barley in a typical endo pattern. With cellulose substrates, the synergism between CBHI and endoglucanase I or II depended on the structural and ultrastructural features of the substrate. This effect, unrelated to endo-exo cooperation, was found with substrates of intermediate crystallinity whereas weak or no synergism was recorded with cellulose microcrystals or the soluble carboxy-methyl cellulose derivative. Synergistic degradation of cellulose was also recorded with mixtures of CBHI and CBHII. On the other hand, synergism between endoglucanases and CBHII followed the pattern expected for an endo-exo cooperation. These results presented support evidence for multiple types of cooperation between the cellulolytic enzymes. 30 references, 7 figures, 1 table.

Authors:: Henrissat, B; Driguez, H; Viet, C; Schuelein, M

Publication Date:: Thu Aug 01 00:00:00 EDT 1985

Research Org.:: Scientific and Medical Univ., Grenoble, Sant-Martin-d'Heres, France

OSTI Identifier:: 5465674

Resource Type:: Journal Article

Journal Name:: Bio/Technology; (United States)

Additional Journal Information:: Journal Volume: 3:8

Country of Publication:: United States

Language:: English

Subject:: 09 BIOMASS FUELS; CELLULASE; CELLULOLYTIC ACTIVITY; SYNERGISM; CELLULOSE; ENZYMATIC HYDROLYSIS; EXPERIMENTAL DATA; MIXTURES; SUBSTRATES; TRICHODERMA VIRIDE; CARBOHYDRATES; CHEMICAL REACTIONS; DATA; DECOMPOSITION; DISPERSIONS; ENZYME ACTIVITY; ENZYMES; FUNGI; GLYCOSYL HYDROLASES; HYDROLASES; HYDROLYSIS; INFORMATION; LYSIS; NUMERICAL DATA; O-GLYCOSYL HYDROLASES; ORGANIC COMPOUNDS; PLANTS; POLYSACCHARIDES; SACCHARIDES; SOLVOLYSIS; TRICHODERMA; 090222* - Alcohol Fuels- Preparation from Wastes or Biomass- (1976-1989); 140504 - Solar Energy Conversion- Biomass Production & Conversion- (-1989)

Citation Formats


                    Henrissat, B, Driguez, H, Viet, C, and Schuelein, M. Synergism of cellulases from Trichoderma reesei in the degradation of cellulose.  United States: N. p., 1985. 
        Web.  doi:10.1038/nbt0885-722.

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                    Henrissat, B, Driguez, H, Viet, C, & Schuelein, M. Synergism of cellulases from Trichoderma reesei in the degradation of cellulose.  United States.  https://doi.org/10.1038/nbt0885-722

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                    Henrissat, B, Driguez, H, Viet, C, and Schuelein, M. 1985.  
        "Synergism of cellulases from Trichoderma reesei in the degradation of cellulose".  United States.  https://doi.org/10.1038/nbt0885-722.

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@article{osti_5465674,

  title        = {Synergism of cellulases from Trichoderma reesei in the degradation of cellulose},

  author       = {Henrissat, B and Driguez, H and Viet, C and Schuelein, M},

  abstractNote = {The action of cellobiohydrolases I and II (CBHI and CBHII) and endoglucanases I and II (EGI and EGII) purified from Trichoderma reesei was evaluated against various substrates. CBHI degraded the ..beta..-D-glucan from barley in a typical endo pattern. With cellulose substrates, the synergism between CBHI and endoglucanase I or II depended on the structural and ultrastructural features of the substrate. This effect, unrelated to endo-exo cooperation, was found with substrates of intermediate crystallinity whereas weak or no synergism was recorded with cellulose microcrystals or the soluble carboxy-methyl cellulose derivative. Synergistic degradation of cellulose was also recorded with mixtures of CBHI and CBHII. On the other hand, synergism between endoglucanases and CBHII followed the pattern expected for an endo-exo cooperation. These results presented support evidence for multiple types of cooperation between the cellulolytic enzymes. 30 references, 7 figures, 1 table.},

  doi          = {10.1038/nbt0885-722},

  url          = {https://www.osti.gov/biblio/5465674},
  journal      = {Bio/Technology; (United States)},
number       = ,

  volume       = 3:8,

  place        = {United States},

  year         = {Thu Aug 01 00:00:00 EDT 1985},

  month        = {Thu Aug 01 00:00:00 EDT 1985}

}

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