Zur Wechselwirkung zwischen einer Penicillium‐Cellulase und wasserlöslichen Cellulosederivaten

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Abstract
Employing anionic and non‐ionic cellulose ethers, differing in type of substituent and degree of substitution, as substrates, the pH‐profile of enzyme activity and the parameter Km and Vmax of the MICHAELIS‐MENTEN kinetics have been determined with Penicillium citrioviride cellulase in an homogeneous system. Within rather wide limits, a linear correlation was found between the DS of the substrate and Km or Vmax, respectively. Also the pH‐profile was found to depend on DS mainly, being bimodal at higher DS. On the other hand, no significant difference was observed between anionic and non‐ionic cellulose ethers of about the same DS with regard to the parameters determined. It is assumed, that substrate‐enzyme interaction is governed mainly by the length of non‐derivatized chain sequences mainly and not by Coulomb interactions.