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. 1969 Nov;115(3):457–464. doi: 10.1042/bj1150457

The cellulase of Fusarium solani. Resolution of the enzyme complex

T M Wood 1
PMCID: PMC1185124  PMID: 5389535

Abstract

1. Culture filtrates from Fusarium solani were fractionated by ion-exchange chromatography on DEAE-Sephadex, followed by gel chromatography on Sephadex G-100, into a C1 component, a Cx component (CM-cellulase) and a β-glucosidase (cellobiase) component. 2. The individual components showed little capacity for the solubilization of cotton fibre (cellulase activity), but when recombined in their original proportions 81% of the original cellulase activity was recovered. 3. The C1 components of F. solani and Trichoderma koningii were similar in their pH optima, heat stabilities over the pH range 5–8 and elution volumes on Sephadex G-100. 4. The C1 component of F. solani synergized with the Cx component of T. koningii and conversely. 5. The C1 and the β-glucosidase components of F. solani were devoid of the swelling-factor (S-factor) activity associated with the Cx component.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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