PURIFICATION AND DETERMINATION OF THE ACTION PATTERN OF HALIOTIS-TUBERCULATA LAMINARINASE

The major laminarinase activity (EC 3.2.1.39) from the gastropodean ma rine mollusc Haliotis tuberculata was purified to homogeneity by catio n exchange chromatography and its action pattern was investigated by H PAEC-PAD analysis off the degradation of various laminarin samples. It consists of a 60 kDa protein capable of depolymerizing the unbranched portions of the beta-(1-->3), beta-(1-->6)-glucan, down to laminaritr iose. The enzyme operates via a molecular mechanism retaining the anom eric configuration. As the purified protein does not cleave the beta-( 1-->6) linkages, it can be used for the structural analysis of laminar ins. (C) 1998 Elsevier Science Ltd. All rights reserved.