Characterization of Cellulases and Related Enzymes by Isoelectric Focusing, Gel Filtration, and Zone Electrophoresis. I. Aspergillus Enzymes.

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Abstract
Physico-chemical characterization has been carried out on the enzymes cellulase, mannase, xylanase, [beta]-glucosidase, aryl-[beta]-glucosidase, mannosidase, and xylosidase from "Cellulase 36", a commercial preparation of Aspergillus enzymes obtained from Rohm and Haas Co. By the iso-electric focusing method the isoelectric points of the enzymes were found to be in the range 3.9-4.7. By gel filtration the relationships between the molecular sizes of the enzymes were estimated. It was found that the extracellular endoenzymes cellulase, mannanase, and xylanase, i.e. those capable by hydrolyzing insoluble high molecular polysaccharides, are smaller molecules than their corresponding exoenzymes which bring about hydrolysis of soluble oligosac-charides. The heterogeneities of the enzymes observed by zone electrophoresis were less pronounced than those observed by the isoelectric focusing method. The reasons for the apparent heterogeneities of the enzymes as indicated by the 3 separation methods that were studied are discussed.