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.
Showing posts with label Aspergillus costaricaensis CBS115574. Show all posts
Showing posts with label Aspergillus costaricaensis CBS115574. Show all posts
Saturday, January 11, 2020
PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR LIPASE ENZYME FROM Aspergillus costaricaensis CBS115574
OPTIMIZATION OF CULTURAL PARAMETERS OF Aspergillus costaricaensis CBS115574 FOR LIPASE PRODUCTION BY SOLID-STATE FERMENTATION
In the present study,
Aspergillus costaricaensis CBS115574 which was previously isolated from the
non-leguminous field soil collected from the Kishangarh city of state Rajasthan
confirmed by 16S rRNA gene/ITS/D1-D2 region sequencing. The cultural parameters
(Carbon sources, nitrogen sources, moisture content, pH, temperature and
particle size etc) of solid-state fermentation have been optimized for the
improved extracellular lipase production. Among different carbon sources, A.
costaricaensis showed best lipase activity (253.6 IU/g/min) in the presence of
lactose. Among the various concentration (0.2%, 0.4%, 0.6%, 0.8%, 1.0%, 1.2%,
1.4% and 1.6%) of lactose, the optimum concentration was found to be 1.6%.
Among different nitrogen sources, highest lipase activity (55.32 IU/g/min) was
obtained in the presence of yeast extract and the optimum concentration of
yeast extract was found to be 0.5% for maximum lipase activity (236.69 IU/g).
Further the best lipase activity was obtained in the medium of pH 8.0 (312.330
IU/g/min) at 28ºC after 48 hrs of incubation period. Further the particle size
of solid substrate was optimized and highest lipase activity was found when
fine particle size was used. Among the various ratio of moisture content,
highest lipase activity (317.09 IU/g/min) was found at 1:6 moisture content.
From the present work, it is figure out that for the enhanced production of
lipases the medium parameters required to be optimized. The above results help
out the authors in carry out the further studies of purification and
characterization of lipase enzyme produced from A. costaricaensis CBS115574.
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