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 <i>Tapes literata</i>. 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 <i>K</i>m 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 <i>T. literata </i>was sequenced and the amino acid sequence was determined. The 13  D glucanase from <i>T. literata </i>was assigned to glycoside hydrolase family 16 (GHF 16).