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International Journal of Current Microbiology and Applied Sciences (IJCMAS)
IJCMAS is now DOI (CrossRef) registered Research Journal. The DOIs are assigned to all published IJCMAS Articles.
Index Copernicus ICI Journals Master List 2019 - IJCMAS--ICV 2019: 96.39 For more details click here
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National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2020)
[Effective from January 1, 2020]
For more details click here

ICV 2019: 96.39
Index Copernicus ICI Journals Master List 2019 - IJCMAS--ICV 2019: 96.39
For more details click here

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Original Research Articles

PRINT ISSN : 2319-7692
Online ISSN : 2319-7706
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcmas@gmail.com / submit@ijcmas.com
Editor-in-chief: Dr.M.Prakash
Index Copernicus ICV 2018: 95.39
NAAS RATING 2020: 5.38

Int.J.Curr.Microbiol.App.Sci.2021.10(4): 232-245
DOI: https://doi.org/10.20546/ijcmas.2021.1004.023


Immobilization Optimization and Characterization of Immobilized Lipase from Lysinibacillus macroides FS1 for Biodiesel Production
Shilpa K. Jigajinni* and Bharati S. Meti
Department of Biotechnology, Basaveshwar Engineering College, S. Nijalingappa Vidyanagar, Bagalkot 587103, Karnataka, India
*Corresponding author
Abstract:

Enzyme Immobilization favours operational stability, reuse, easy separation and enhanced stability than free enzyme. Lipase from Lysinibacillus macroides FS1 was entrapped into Ca-alginate gel beads and effect of independent variables such as alginate concentration of 1-4% (w/v) and CaCl2 concentration of 50-200mM on immobilization efficiency and activity were investigated. After optimization of immobilization conditions, maximum immobilization efficiencies of 69% and activity of immobilized lipase was 6.0 U/ml were recorded at optimum concentrations of 4% (w/v) sodium alginate and 200mM CaCl2. The optimum temperature of both free and immobilized lipase was 45°C and optimum pH of free and immobilized lipase was pH 5 and 8 respectively. The lipase activity of 46% was recovered by immobilized lipase after 6 cycles of reusability. Stability studies revealed that immobilized lipase was more stable than free lipase at optimum pH (8) and temperature (45°C) when incubated for 3 hr. Furthermore, the immobilized lipase showed enhanced stability to methanol than ethanol compared to free lipase. The biodiesel was produced by using immobilized lipase and it was confirmed by glycerol assay. These findings advise the efficient and sustainable use of the developed immobilized lipase as a biocatalyst for production of biodiesel.


Keywords: Lysinibacillus macrolides FS1, Ca-alginate beads, Stability, Reusability, Fatty acid methyl ester
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How to cite this article:

Shilpa K. Jigajinni and Bharati S. Meti. 2021. Immobilization Optimization and Characterization of Immobilized Lipase from Lysinibacillus macroides FS1 for Biodiesel ProductionInt.J.Curr.Microbiol.App.Sci. 10(4): 232-245. doi: https://doi.org/10.20546/ijcmas.2021.1004.023