2009 Volume 56 Issue 1 Pages 13-16
1,4-β-Endoglucanase was purified from the hepatopancreas of the marine mollusc, Patinopecten yessoensis, by cellulose column chromatography. The enzyme (EG66) showed the Mr of 66K on SDS-PAGE, and the hydrolytic activity was maximal at pH 6.0. EG66 readily hydrolyzed glucomannan and β-1,3-1,4-glucan as well as CMC and hydroxyethyl cellulose. On the other hand, crystalline cellulose, xylan, xyloglucan, laminarin, β-1,3-1,6-glucan, galactomannan, alginate, methyl cellulose and hydroxypropylmethyl cellulose were not hydrolyzed at all. N-Terminal amino acid sequence of EG66, which was determined as GATNVQIT NEWPGGFQGTF, had a motif common to the other molluscan endoglucanases.