CATALYTIC PROPERTIES AND AMINO ACID SEQUENCE OF ENDO-13--D-GLUCANASE FROM THE MARINE MOLLUSK <i>Tapes literata</i>
A specific 13  D glucanase with a molecular mass of 37.0 kDa was isolated in the homogeneous state from crystalline styles of the commercial marine mollusk Tapes literata. It displayed the maximal activity within the pH range 4.5 to 7.5 and temperature 45°C. The 13  D glucanase catalyzes hydrolysis of 1,3 bonds of glucans as an endoenzyme with retention of bond configuration and possesses transglycosylating activity. The Km values of the 13  Dglucanase is 0.25 mg/ml in the reaction with laminaran. The enzyme is classified as a glucan endo (13)  D glucosidase (EC 3.2.1.39). The cDNA encoding 13  D glucanase from T. literata was sequenced and the amino acid sequence was determined. The 13  D glucanase from T. literata was assigned to glycoside hydrolase family 16 (GHF 16).