Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2012 Jan;43(1):30-42.
doi: 10.1590/S1517-83822012000100004. Epub 2012 Jun 1.

Optimization of extracellular thermophilic highly alkaline lipase from thermophilic bacillus sp isolated from hotspring of Arunachal Pradesh, India

Limpon Bora  1 , Minakshi Bora
Affiliations

Optimization of extracellular thermophilic highly alkaline lipase from thermophilic bacillus sp isolated from hotspring of Arunachal Pradesh, India

Limpon Bora et al. Braz J Microbiol. 2012 Jan.

Abstract

Studies on lipase production were carried out with a bacterial strain (Bacillus sp LBN 2) isolated from soil sample of hotspring of Arunachal Pradesh, India. The cells were cultivated in a mineral medium with maximum production at 1% groundnut oil. The optimum temperature and initial medium pH for lipase production by the organism were 50(0)C and 9.0 respectively. The molecular mass was found to be 33KDa by SDS PAGE. The optimal pH and temperature for activity were 10 and 60(0)C respectively. The enzyme was found to be stable in the pH range of 8-11 with 90% retention of activity at pH 11. The enzyme retained 90% activity at 60(0)C and 70% of activity at 70(0)C for 1h. The lipase was found to be stable in acetone followed by ethanol. The present findings suggested the enzyme to be thermophilic alkaline lipase.

Keywords: Alkaline lipase and Bacillus sp; Thermophilic bacteria; Thermostable.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Time course of lipase production. The values are mean ± SD of three replicates.
Figure 2
Figure 2
Each value represents the mean of ± standard errors values with no common letter in column are significantly different at p< 0.05.
Figure 3
Figure 3
Each value represents the mean of ± standard errors values with no common letter in column are significantly different at p< 0.05.
Figure 4
Figure 4
The effect of temperature on lipase production. The values are mean + SD of three replicates. –––■–– Activity (U/ml) –––◆–– (Protein (mg/ml)
Figure 5
Figure 5
The Effect of pH on lipase production. The values are mean + SD of three replicates. –––■–– Protein (mg/ml)–––◆––(Activity (U/ml)
Figure 6
Figure 6
Effect of Salt Concentration on lipase production
Figure 7
Figure 7
Gel showing the purified lipase. Lane 1. Lipase protein (investigated) Lane 2 Standard protein markers phosphorylase b (97.4 KDa), Fructose 6 phosphate kinase (84KDa), bovine serum albumin (68KDa), Glyceraldehyde 3 phosphate dehydogenase (36KDa), Trypsinogen (24 KDa), β Lactoalbumin (14.2KDa).
Figure 8
Figure 8
Effect of pH on activity and stability.
Figure 9
Figure 9
Effect of temperature on activity and stability
See this image and copyright information in PMC

References

    1. Abdel-Fattah Y.R. Optimization of thermostable lipase production from a thermophilic Geobacillus sp. using Box-Behnken experimental design. Biotechnol Lett. 2002;24:1217–1222.
    1. Ateslier Z.B.B., Metin K. Production and partial characterization of novel thermostable esterase from a thermophilc Bacillus sp. Enzyme Microb Technol. 2006;38:628–635.
    1. Baral A., Fox P.F. Isolation and characterization of an extracellular lipase from Pseudomonas tolaassi. Fd.. Chem. 1997;58:33–38.
    1. Bayoumi R.A., El-louboudey S.S., Sidkey N.M., Abd-El-Rahman M.A. Production, Purification and Characterization of Thermoalkalophilic Lipase for Application in Bio-detergent Industry. J. Apll. Sci. Res. 2007;3:1752–1765.
    1. Boekema K.H.A., Beselin M., Breuer B., Hauer M., Koster F., Rosenau K., Tommassen J. Hexadecane and Tween 80 stimulate lipase production in Burkholderis glume by different mechanisms. Appl. Environ. Microbiol. 2007;73:3838–3844. - PMC - PubMed

LinkOut - more resources