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Title: Studies on component C2 of the cellulase complex
Author: Jones, J. E.
Awarding Body: University College of Swansea
Current Institution: Swansea University
Date of Award: 1979
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The cellulolytic enzyme complex of Humicola insolens has been fractionated, by column chromatography, into four components: (i) cellobiase (ii) a CM-cellulase (iii) component C1 and (iv) component C2. A scheme was devised for the isolation of component C2 relatively free from its main contaminant, CM-cellulase. In this scheme the fractionation of concentrated culture filtrate by chromatography on columns of cellulose powder was followed by repeated fractionation on columns of DEAL cellulose. The C2 component so isolated released a range of products from bacterial cellulose and, less extensively, from cotton. These products were glucose and a range of cellodextrins up to cellopentose. The cellotriose, cellotettose and cellopentose were degraded to glucose and cellobiose in the presence of CM-cellulase. Component C2 also attacked insoluble dextrins and short fibres but not glucose, cellobiose or cellotriosz. The main products from cotton were short fibres, but these were not extensively produced by purified component C2 unless CM-cellulase was added. The purified component C2 was unstable and the synergistic response with CM-cellulase could be achieved by replacing CM-cellulase with bovine serum albumin. Swelling-factor (S-factor) activity was a property of both component C2 and CM-cellulase. Short fibre formation was decreased in the absence of oxygen but the formation of soluble products from cotton or bacterial cellulose was not affected. Short fibre formation was inhibited by CM-cellulase but not much by glucose or cellobiose. The interrelationship of these effects is discussed and a scheme for the solubilisation of cotton is given.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available