The chromatographic analysis of the enzyme cellulose
Glennon, William Edward
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This thesis attempted to give further evidence to the multiple component theory of the enzyme cellulase as well as presenting methods of purifying the enzyme. Cellulase was prepared in this laboratory from Myrothecium verrucaria. Batch absorption experiments using cellulose as adsorbent showed that 30% of the activity and protein could be adsorbed at pH 5 with acetate buffer. A very dilute salt concentration as 0.0001 M NaCl allowed 58% adsorption of activity in the batch adsorption experiments with cellulose. The long cellulose chromatographic column adsorbed irreversibly 100% of the activity allowing the protein and carbohydrate to be eluted. The column of cellulose must be permitted more sites for the enzyme to absorb to than just placing the enzyme in the cellulose and mixing. The short cellulose columns showed the presence of a readily absorbed component as well as a less readily absorbed component. [TRUNCATED]
Thesis (M.A.)--Boston University
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