Abstract
The cellulase enzyme complex can be immobilized quite easily by covalent attachment to water-soluble and insoluble supports and by entrapment within gel matrices. Fungal mycelia that are secreting cellulase can also be immobilized for the continuous production of cellulase. Cellulase that has been immobilized to water-soluble polymers is capable of hydrolyzing insoluble cellulosic substrates, but alterations in the specific activity or stability of the enzyme have not been evident. When immobilized by entrapment or by covalent attachment to water-insoluble supports, limited hydrolysis of cellulosic substrates by such immobilized cellulases is possible. The β-glucosidase component of cellulase can be stabilized and immobilized for efficient hydrolysis of soluble cellobiose and short-chain cello-oligosaccharides.
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