| Autor: |
Zakharenko AM, Kusaĭkin MI, Li BM, Huen FV, Khan HH, Sova VV, Zviagintseva TN |
| Jazyk: |
ruština |
| Zdroj: |
Bioorganicheskaia khimiia [Bioorg Khim] 2009 Jan-Feb; Vol. 35 (1), pp. 62-9. |
| DOI: |
10.1134/s1068162009010075 |
| Abstrakt: |
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 45 degrees C. Its half-inactivation time is 180 min at 45 degrees C and 20 min at 50 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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