ABSTRACT
An early result observed with exochitinase activity showed that exoenzymes require access to free ends of chitin assemblies, irrespective of whether the enzymes are derived from procaryotic or eucaryotic sources. Using Linear Chitin in enzyme studies, separate assays for exo- and endochitinase activity were formulated. A log-log conversion of velocity versus substrate concentration for exochitinase derived from molting fluid was compared with one constructed with similar data obtained for a Streptomyces-derived exochitinase. Chitinase from the yeast species Saccharomyces cerevisiae shows some sequence identity to chitinases from a variety of microorganisms, endo-H enzyme from S. plicatus, and a yeast killer toxin from a Kluyveromyces species. The capacity for producing chitinases and chitosanases by microorganisms upon encountering chitin and/or chitosan was demonstrated by Eveleigh and co-workers for organisms in “any soil or sediment examined”. Chitinases from microorganisms demonstrably are simple hydrolases.
