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• W2021657414 abstract "The C1 component from Fusarium solani cellulase was purified extensively by molecular-sieve chromatography on Ultrogel AcA-54 and ion-exchange chromatography on DEAE-Sephadex. The purified component showed little capacity for hydrolysing highly ordered substrates (e.g., cotton fibre), but poorly ordered substrates (e.g., H3PO4-swollen cellulose), and the soluble cello-oligosaccharides cellotetraose and cellohexaose, were readily hydrolysed; cellobiose was the principal product in each case. Attack on O(-carboxymethyl)cellulose, a substrate widely used for measuring the activity of the randomly acting enzymes (Cx enzymes) of the cellulase complex, was minimal, and ceased after the removal of a few unsubstituted residues from the end of the chain. These observations, and the fact that the rate of change of degree of polymerisation of H3PO4-swollen cellulose was very slow compared with that effected by the randomly acting endoglucanases (Cx, CM-cellulases), indicate that C1 is a cellobiohydrolase. Fractionation by a variety of methods gave no evidence for the non-identity of the cellobiohydrolase and the component that acted in synergism with the randomly acting Cx enzyme when solubilizing cotton fibre." @default.
• W2021657414 created "2016-06-24" @default.
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• W2021657414 date "1977-08-01" @default.
• W2021657414 modified "2023-09-27" @default.
• W2021657414 title "Cellulase from Fusarium solani: Purification and properties of the C1 component" @default.
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• W2021657414 doi "https://doi.org/10.1016/s0008-6215(00)81925-4" @default.
• W2021657414 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/409496" @default.
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