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Activity of Immobilized Pronase in the Presence of Montmorillonite¹

ABSTRACT

The activity of soluble and immobilized pronase in the presence of montmorillonite was examined using a differential spectrophotometric technique over a 100-sec incubation period. On the basis of equivalent amounts of enzyme protein, the immobile enzyme had only 28% of the activity of the soluble pronase in the absence of clay. However, in the presence of clay, the immobile pronase was much less inhibited, retaining an average of 75% of its activity while the soluble pronase retained only 31% of its activity. The differential spectrophotometric procedure was satisfactory for monitoring the enzyme action in the presence of suspended clay.

¹ Contribution from the Department of Land Resource Science, University of Guelph, Guelph, Ontario, N1G 2W1.

² Research Assistant and Professor, respectively.

Received for publication January 9, 1978. Accepted for publication July 6, 1979.