[Catalytic properties of endo-1,3-beta-D-glucanase from the Vietnamese edible mussel Perna viridis].
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.
A M
AM
Zakharenko
M I
MI
Kusaĭkin
Bui Min
BM
Li
Fam Van
FV
Huen
Hyun Hoang
HH
Khan
V V
VV
Sova
T N
TN
Zviagintseva
D000818:Animals; D002384:Catalysis; D043326:Glucan 1,3-beta-Glucosidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D005936:Glucans / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D049879:Mytilidae / Q000201:enzymology*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013379:Substrate Specificity; D014744:Vietnam
D005936:Glucans; D043326:Glucan 1,3-beta-Glucosidase