Abstract
This paper presents the influence of pH on the activity and stability of an extracellular chitin deacetylase produced by Absidia orchidis. It showed the highest activity at pH 4.0 and was most stable at pH 9.5. In addition, there was pH deactivation that could be described by first-order irreversible kinetics. The pH deactivation rate constant changed linearly with pH in the range from 4.0 to 9.0.
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