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J. Biol. Chem., Vol. 265, Issue 13, 7207-7215, 05, 1990
Y Tsumuraya, N Mochizuki, Y Hashimoto and P Kovac
An exo-beta-(1----3)-D-galactanase from Driselase, a commercial enzyme
preparation from Irpex lacteus (Polyporus tulipiferae) has been purified
166-fold. Apparent molecular weights of the purified enzyme, estimated by
denaturing gel electrophoresis and gel filtration, were found to be 51,000
and 42,000, respectively. It hydrolyzed specifically oligosaccharides and
polymers of (1----3)-linked beta-D- galactopyranosyl residues, and
exhibited a maximal activity toward these substrates at pH 4.6. Based on
the mode of the liberation of D- galactose from beta-(1----3)-D-galactan
and the methyl beta-glycoside of beta-(1----3)-D-galactopentaose, the
enzyme can be classified as an exo-glycanase capable of catalyzing the
sequential hydrolytic release of single D-galactosyl residues from the
nonreducing termini. The extent of the hydrolysis of the carbohydrate
portion of acacia gum and radish arabinogalactan-proteins increased with
their decreasing branching. Isolation and characterization of the major
products formed from the proteoglycans indicated the action pattern of the
enzyme to include the capability of bypassing the branching points.
Consequently, the side chains carrying an additional D-galactosyl group at
the reducing termini are released as neutral (1----6)-linked beta-D-
galactooligosaccharides and their acidic derivatives having a 4-O-
methyl-beta-D-glucuronosyl residue as the nonreducing end-group. The
specificity and the mode of action showed the enzyme to be a useful tool
for analyzing the fine structure of type II arabinogalactans and
arabinogalactan-protein conjugates.
Purification of an exo-beta-(1----3)-D-galactanase of Irpex lacteus (Polyporus tulipiferae) and its action on arabinogalactan-proteins
Department of Biochemistry, Faculty of Science, Saitama University, Urawa, Japan.
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