Abstract
Some physicochemical properties and substrate specificity of acid protease B isolated from Scytalidium lignicolum were investigated.
The molecular weight determined by the sedimentation equilibrium and sedimentation velocity method was 21, 000 and 19, 000_??_20, 000, respectively. The isoelectric point was determined as 3.0 using the Tiselius electrophoresis apparatus, 3.2 by isoelectric focusing, respectively.
The enzyme did not contain histidine and was composed of 188 amino acid residues.
Substrate specificity against various synthetic peptides was different from those of the acid proteases which were inactivated by S-PI and DAN.
