Chitinase and beta-N-Acetylglucosaminidase in the Digestive Juice of Helix pomatia.

Abstract

.beta.-N-acetylglucosaminidase from H. pomatia digestive juice was separated and partly purified by gel chromatography. The optimal pH for the degradation of p-nitrophenyl-N-acetyl-.beta.-D-glucosaminide was 3.4. The MW was .apprx. 160,000 and the pI [isoelectric point] = 4.95. In the same chromatography run 2 chitinase active peaks were also obtained. These chitinases with MW .apprx. 26,000 and 13,000, had somewhat different pH activity curves with optima at 4.2 and 4.3. By isoelectric focusing the 1st peak with MW .apprx. 26,000 was divided in 2 chitinase active regions with pI at 5.7 and 3.8. The 2nd peak with MW .apprx. 13,000 had a pI at 7.3.