| dc.description.abstract |
An alkaline protease from marine Engyodontium
album was characterized for its physicochemical
properties towards evaluation of its suitability for potential
industrial applications. Molecular mass of the enzyme by
matrix-assisted laser desorption ionization-mass spectrometry
(MALDI-MS) analysis was calculated as 28.6 kDa.
Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by
phenylmethylsulfonyl fluoride (PMSF) and aprotinin
confirmed the serine protease nature of the enzyme.Km, Vmax,
and Kcat of the enzyme were 4.727 9 10-2 mg/ml,
394.68 U, and 4.2175 9 10-2 s-1, respectively. Enzyme
was noted to be active over a broad range of pH (6–12) and
temperature (15–65 C), withmaximumactivity at pH 11 and
60 C. CaCl2 (1 mM), starch (1%), and sucrose (1%) imparted
thermal stability at 65 C. Hg2?, Cu2?, Fe3?, Zn2?, Cd?, and
Al3? inhibited enzyme activity, while 1 mMCo2? enhanced
enzyme activity. Reducing agents enhanced enzyme activity
at lower concentrations. The enzyme showed considerable
storage stability, and retained its activity in the presence of
hydrocarbons, natural oils, surfactants, and most of the
organic solvents tested. Results indicate that the marine
protease holds potential for use in the detergent industry and
for varied applications. |
en_US |