Partial purification and properties of lipase from germinating seeds of Jatropha curcas L.

Abigor, R. D.; Uadia, Patrick; Foglia, Thomas A.; Haas, Michael J.; Scott, Karen M.; Savary, Brett J.

doi:10.1007/s11746-002-0614-3

Cited by 52 publications

(44 citation statements)

References 18 publications

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“…Seed lipases from Jatropha curcas L., also known as Barbados nut, were studied by Abigor et al (2002). The lipase was partially purified using a combination of ammonia sulphate precipitation and ultrafiltration.…”

Section: Barbados Nut Lipases (Jatropha Curcas L)mentioning

confidence: 99%

Seed lipases: sources, applications and properties - a review

Barros

Fleuri

Macêdo

2010

Braz. J. Chem. Eng.

178

100

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-This paper provides an overview regarding the main aspects of seed lipases, such as the reactions catalyzed, physiological functions, specificities, sources and applications. Lipases are ubiquitous in nature and are produced by several plants, animals and microorganisms. These enzymes exhibit several very interesting features, such as low cost and easy purification, which make their commercial exploitation as industrial enzymes a potentially attractive alternative. The applications of lipases in food, detergents, oils and fats, medicines and fine chemistry, effluent treatment, biodiesel production and in the cellulose pulp industry, as well as the main sources of oilseed and cereal seed lipases, are reviewed.

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Section: Barbados Nut Lipases (Jatropha Curcas L)mentioning

confidence: 99%

Seed lipases: sources, applications and properties - a review

Barros

Fleuri

Macêdo

2010

Braz. J. Chem. Eng.

178

100

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“…In others works from the literature, Enujiugha et al (2004) found that Calcium ion in the reaction mixture brought about 64% increase in activity of lipase activity in dormant seeds. Abigor et al (2002) and Haas et al (1992) also observed an enhancement of lipase activity by calcium ion inclusion. From the work of Mukundan et al (1985), the chloride ion did not cause any inhibitory effect but the metal ions (Na + , Hg 2+ ) enhanced lipase decrease.…”

Section: Na = Not Availablementioning

confidence: 87%

Catalytic properties of lipase from Ficus trichopoda and Euphorbia unispina latex: Study of their typoselectivity

Mazou¹,

Djossou²,

Tchobo³

et al. 2017

J. App. Bioscience.

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Objective: The search for lipase with distinct features, from plant latex is of great importance for industrial applications. The catalytic properties of lipases from Ficus trichopoda and Euphorbia unispina latex were characterized. Methodology and Results: Fresh latex from Ficus trichopoda and Euphorbia unispina were collected and dried through solar. Dried latex was taken for complete proximate analysis and their activity was analysed by thin layer chromatography. The two lipases were optimally active at pH=5 and temperature of 35°C and 50°C for Ficus trichopoda and Euphorbia unispina latex, respectively. The presence of metal ions enhances the activity of Ficus trichopoda latex, while no significant enhancement was observed in the case of Euphorbia unispina latex. Both lipases were able to hydrolyze saturated esters, and showed typo-selectivity for this group. However, the lipases are weak selective for the hydrolysis of unsaturated esters, especially for 18:2 fatty acids. Conclusions and application of finding: The enzyme from Ficus trichopoda latex was able to attack specific oil to generate free fatty acids or ester as the major product. This understanding may help in devising efficient methods to produce valuable modified oils.

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“…The purification process resulted in 2.8-fold purification and a final yield of 80% of the enzyme with a specific activity of 940 U/mg. Abigor et al, (2002) [19] also reported that the lipase enzyme produced from Jatropha curcas purified with 80% ammonium sulfate precipitation achieved a 2.8-fold increase in the relative activity of the lipase in the supernatant.…”

Section: Ammonium Sulfate Purification Of Lipase Enzymementioning

confidence: 93%

Isolation, Purification, and Characterization of Lipase From Bacillus Sp. From Kitchen Grease

Jaiganesh

2018

Asian J Pharm Clin Res

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Objective: The objective of this work was to isolation, purification and characterization of solvent tolerant lipase from Bacillus sp. The objective of this work was to isolation, purification and characterization of solvent tolerant lipase from Bacillus sp. from kitchen grease for a variety of applications including organic synthetic reactions and preparation of enantiomerically pure pharmaceuticals.Methods: Lipase producing isolates were screened from kitchen grease on a selective medium rhodamine B olive oil agar, and tributyrin agar was used to screen the lipase and esterase producing an organism, respectively. The isolate identified using 16S rDNA sequencing method and enzyme activity was quantitatively assayed. Lipase production was characterized in different conditions. Results:The isolate showed highest lipase activity was which later was identified as Bacillus sp. using 16S rDNA sequencing method. The lipase was purified using ammonium sulfate precipitation. The isolate showed excellent tolerance to methanol, ethanol, acetonitrile, and moderate tolerance to butanol. The increased biomass concentration, maximum production, and activity were achieved at 37°C in 24 h incubation, then gradual reduction in production was observed. The maximum activity of lipase enzyme was obtained at pH between 6 and 9. Conclusion:The isolate produce solvent tolerance lipase enzyme and it can be a promising candidate of solvent tolerance lipase enzyme for variety of industrial applications.

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Partial purification and properties of lipase from germinating seeds of Jatropha curcas L.

Cited by 52 publications

References 18 publications

Seed lipases: sources, applications and properties - a review

Seed lipases: sources, applications and properties - a review

Catalytic properties of lipase from <i>Ficus trichopoda</i> and <i>Euphorbia unispina</i> latex: Study of their typoselectivity

Isolation, Purification, and Characterization of Lipase From Bacillus Sp. From Kitchen Grease

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