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Prikl Biokhim Mikrobiol ; 18(4): 581-7, 1982.
Article in Russian | MEDLINE | ID: mdl-6812038

ABSTRACT

The activity of beta-mannanase from Bacillus subtilis was measured viscosimetrically and spectrophotometrically. As substrate galactomannane of Ceratonia siliqua was used. Relationships between the beta-mannanase activity and the substrate concentration as well as the enzyme content were investigated. The kinetic parameters of the enzymes obeying the Michaelis-Menten equation were calculated. It was found viscosimetrically that Vmax of the commercial enzyme preparation was 1.4 mucat/g (at pH 5.8 and 40 degrees) and Km was 0.6 mM. The viscosimetric method shows high sensitivity, whereas the spectrophotometric technique suits mass-scale analyses.


Subject(s)
Mannosidases/analysis , Spectrophotometry/methods , Bacillus subtilis/enzymology , Dose-Response Relationship, Drug , Kinetics , Viscosity , beta-Mannosidase
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