Isolation of two endo-β-N-acetylglucosaminidases from fig latex

Two endo-β-N-acetylglucosaminidases (mannosyl-glycoprotein $\text{1,4-N-}\text{acetamidodeoxy}\text{-β-}\text{d}\text{-}\text{glycohydrolase}$, EC 3.2.1.96) (type F-I and type F-II) have been isolated from fig latex. At pH 7.0, type F-1 was retained by the DEAE-Sephadex A-50 column, whereas type F-II was not adsorbed by the column. The optimum pH of type F-I was found to be pH 5.9 and type F-II, pH 5.4. Type F-I enzyme hydrolyzes the tri-mannosyl derivatives di-N-acetylglucosaminylasparagine faster than the penta- or hexa-mannosyl compounds. Type F-II hydrolyzes the penta- and hexa-mannosyl derivatives, but not the tri-mannosyl compound.