Two beta-1,3-glucanases (I and II) have been isolated from vacuum extr
act of potato leaves. The enzymes have optimum activity at 30 degrees
C and pH 5.5. By gel filtration, the molecular weights of glucanase I
and glucanase II are 22 and 20 kD, respectively. By electrophoresis un
der denaturing conditions, their molecular weights are 30 and 28 kD, r
espectively. Inhibitor analysis indicates that tryptophan and dicarbox
ylic acid residues are important for the activities of glucanases I an
d II. The enzymes are resistant to some natural inhibitors of carbohyd
rases. The two enzymes cleave laminaran as endo-specific enzymes, prod
ucing oligosaccharides with different degree of polymerization and a t
race amount of glucose. Glucanase I has higher viscosimetric activity
towards carboxymethylpachyman than glucanase II. The enzymes have tran
sglycosylating activity. This capability is probably used in the plant
s for the synthesis of elicitors initiating a protection mechanism.