Enzymatic Properties of β-1,3-Glucanase from Streptomyces sp Mo.


Direct inquiries to author Kurakake (E-mail: kurakake@fubac.fukuyama-u.ac.jp)


Streptomyces sp Mo endo-β-1,3-glucanase was found to have hydrolyzing activity toward curdlan and released laminarioligosaccharides selectively. The molecular weight was estimated to be 36000 Da and its N-terminal amino acid sequence was VTPPDISVTN. The optimal pH was 6 and the enzyme was found to be stable from pH 5 to 8. The optimal temperature was 60 °C and the activity was stable below 50 °C. The enzyme hydrolyzed selectively curdlan containing only β-1,3 linkages. The enzyme had 89% relative activity toward Laminaria digitata laminarin, which contains a small amount of β-1,6 linkages compared with curdlan, while Eisenia bicyclis laminarin with a higher amount of β-1,6-linkages, was not hydrolyzed. Mo enzyme adsorbed completely on curdlan powder. The enzymatic hydrolysis of curdlan powder resulted in the accumulation of laminaribiose (yield 81.7%). Trisaccharide was inevitably released from the hydrolysis of laminarioligosaccharides with 5 to 7 degrees of polymerization (DP). Although the enzyme cleaved off disaccharide (DP 2) from tetrasaccharide (DP 4), the reaction rate was lower than those of DP 5 to 7. The results indicated that the active site of Mo endo-β-1,3-glucanase can efficiently recognize glucosyl residue chain of greater than DP 5 and hydrolyzes the β-1,3 linkage between the 3rd and 4th glucosyl residue.