PURIFICATION AND SOME PROPERTIES OF AN ENDO-1,4-BETA-D-MANNANASE FROMA MARINE MOLLUSK, LITTORINA-BREVICULA

An endo-1,4-beta-D-mannanase (EC 3.2.1.78) was purified from viscera o f a marine mollusc, Littorina brevicula. The purified enzyme, with a m olecular weight of 42,000, was homogeneous by SDS-PAGE. The amino-term inal sequence starting with Gly was analyzed up to the 30th amino acid . The enzyme was stable from pH about 4.0 to about 9.0 and had its max imum activity at pH about 6.5. The purified enzyme produced M2, M3, M4 , and M5 from Codium beta-1,4-mannan. The enzyme activity was greatly inhibited by Ag+, Hg2+, Cu2+, and N-bromosuccinimide at 1 mM concentra tion.