In the present study,
the lipase of alkaline nature obtained from the previously isolated strain
Aspergillus costaricaensis CBS115574 was characterized and purified out using
ammonium sulfate precipitation and chromatographic techniques on
Diethylaminoethyl A-50 and Sephadex G-100. The purified lipase has the
molecular weight of ~50 kDa which was determined by Sodium dodecyl sulfate
polyacrylamide gel electrophoresis (SDS-PAGE) and Zymography by using the
phenol red along with the purification fold of 6.63 and specific activity of
31.73 IU/mg after the gel filtration chromatography. Lipase was found to be
stabilized at the pH 7 (122.68 IU/g/min) and at the temperature of 80ºC (141.36
IU/g/min) with its optimal activity at pH 8 and temperature 50ºC. The Km and
Vmax value for extracellular lipase were reported to be 29.62 mM and 74.07
IU/ml with their higher tolerance to glycerol (organic solvent), tween 80
(detergent), Ethylene diamine tetra acetic acid (activator & inhibitor),
hydrogen peroxide (oxidizing & reducing agent) and sodium chloride (metal
ions) with lipase activity of 106.74 IU/g/min, 84.53 IU/g/min, 108.06 IU/g/min,
97.17 IU/g/min and 118.7 IU/g/min. The above results suggested that A.
costaricaensis CBS115574 lipase found a suitable position for application in
different types of industries.
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