期刊
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
卷 35, 期 1, 页码 54-61出版社
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S1068162009010075
关键词
endo-beta-1,3-glucanase; mussel; Perna viridis; crystalline stalk; laminaran
资金
- Russian Foundation for Basic Research [07-04-90010]
- CRDF [REC-003]
- Russian Academy of Sciences Molecular and Cellular Biology
A beta-1,3-glucanase with a molecular mass of 33 kDa was isolated in the homogeneous state from a crystalline stalk of the commercially available Vietnamese edible mussel Perna viridis. It hydrolyzes beta-1,3-bonds in glucans and is capable of catalyzing the transglycosylation reaction. The beta-1,3-glucanase has a K (m) value of 0.3 mg/ml for the hydrolysis of laminaran and shows a maximum activity in the pH range from 4 to 6.5 and at 45A degrees C. Its half-inactivation time is 180 min at 45A degrees C and 20 min at 50A degrees C. The enzyme was ascribed to glucan-endo-(1 -> 3)-beta-D-glucosidases (EC 3.2.1.39). The enzyme could be used in the structure determination of beta-1,3-glucans and enzymatic synthesis of new carbohydrate-containing compounds.
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