Purification and Some Properties of a Novel Endo-β-(1→6)-D-galactanase from Aspergillus niger

Abstract

An endo-β-(1→6)-D-gaIactanase has been purified 26-fold (14% activity yield) from a crude enzyme preparation from Aspergillus niger. The enzyme was homogeneous on PAGE and SDS-PAGE, with an apparent molecular mass of 60 kDa. It has maximum activity at pH 3.5 on an enzymatically desarabinosylated grape 3,6-galactan-protein (Gp), being unreactive towards the native grape AGp. The enzyme liberated β-(1→6)-D-gaIactobiose and galactose in a final 1:0.26 molar ratio, β-(1→3)-D-galactosidic bonds being resistant to the action of enzyme. © 1991, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.