[Chemical modification of lysine residues of beta-1,3-glucanase from Spisula sachalinensis].
The effects of chemical modification of the amino groups of lysine residues on the activity of beta-1.3-glucanase from Spisula sachalinensis were studied. Modification of two lysine residues per molecule did not affect either the enzyme activity with respect to laminarine, nor the Km value. The modified beta-1.3-glucanase retains the ability to catalyze the transglycosylation and cleaves the high molecular weight CM-pachyman at the same rate as does the native enzyme. No significant changes in the enzyme thermal stability were observed. Thus, the modified enzyme groups cannot be involved in the enzyme active center and are exposed on the surface of the protein globule. The chemical modification was shown to have no effect on the enzyme kinetics, which is essential for its immobilization.
D000818:Animals; D001665:Binding Sites; D049872:Bivalvia / Q000201:enzymology*; D004355:Drug Stability; D043326:Glucan 1,3-beta-Glucosidase; D005959:Glucosidases / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine; D013379:Substrate Specificity
D005959:Glucosidases; D043326:Glucan 1,3-beta-Glucosidase; D008239:Lysine
Khimicheskaia modifikatsiia ostatkov lizina v beta-1,3-gliukanaze iz Spisula sachalinensis.