Purification and Characterization of the Lipase from Marine Vibrio fischeri

Ranjitha, P.; Karthy, E.S.; Mohankumar, A.

doi:10.5539/ijb.v1n2p48

Cited by 15 publications

(11 citation statements)

References 29 publications

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“…The results for varying optimum pH coincide with various studies carried out by Mubarak-Qamsari et al [21] which reveal similar results that the enzyme has the ability to work at pH 9 and 10. Thermostability results are similar to such studies carried out on lipase by Ranjitha et al [27] where the enzyme was stable at 30°C while pH stability studies also agree with studies carried out by Annamalai et al [28] who also observed that the lipase from Bacillus licheniformis was stable at pH 9.…”

Section: Discussionsupporting

confidence: 81%

Production and Partial Characterization of Lipase from Pseudomonas putida

Fatima¹,

Khan²

2015

Ferment Technol

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The production of lipase from Pseudomonas putida 922 was optimized by modifying various physical parameters such as carbon source, nitrogen source, pH, salt concentration and biochemical parameters of the production medium such as temperature and incubation time of the growth medium. Oil cakes were also used as carbon source to check for an increased production of the enzyme. The bacterium was found to have a maximal growth at pH 10 with the enzyme production being highest (24 U/ml) after 48 hours at 30°C and pH 10. The optimum composition of the medium was mustard oil cake as carbon source, yeast extract or peptone as nitrogen source and 1% sodium chloride concentration. Partial characterization of the enzyme was carried out where the optimum working pH and temperature was found to be 10 and 40ºC, respectively. Enzyme stability was found to lie in the pH and temperature ranges of 5-11 and 30-40ºC, respectively. Partial purification of the enzyme was carried out at 80% ammonium sulphate saturation. Molecular mass of lipase was determined by SDS PAGE and found to be 45 kDa.

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Section: Discussionsupporting

confidence: 81%

Production and Partial Characterization of Lipase from Pseudomonas putida

Fatima¹,

Khan²

2015

Ferment Technol

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“…Other workers have used ultrafiltration [66,74], acetone precipitation [75], and ethanol precipitation [76]. The next step usually involves the use of dialysis to remove ammonium sulfate traces and other impurities present in the culture medium [77,78]. Further purification is done by chromatographic technique such as gel filtration chromatography, ions exchange chromatography, adsorption chromatography, hydrophobic interaction chromatography or HPLC [68,71,79].…”

Section: Purification Of β-Glucosidasementioning

confidence: 99%

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

Ahmed¹,

Aslam²,

Ashraf³

et al. 2017

JAEM

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Cellulose is the most abundant biomaterial in the biosphere and the major component of plant biomass.Cellulase is an enzymatic system required for conversion of renewable cellulose biomass into free sugar for subsequent use in different applications. Cellulase system mainly consists of three individual enzymes namely: endoglucanase, exoglucanase and β-glucosidases. β-Glucosidases are ubiquitous enzymes found in all living organisms with great biological significance. β-Glucosidases have also tremendous biotechnological applications such as biofuel production, beverage industry, food industry, cassava detoxification and oligosaccharides synthesis. Microbial β-glucosidases are preferred for industrial uses because of robust activity and novel properties exhibited by them. This review aims at describing the various biochemical methods used for screening and evaluating β-glucosidases activity from microbial sources. Subsequently, it generally highlights techniques used for purification of β-glucosidases. It then elaborates various biochemical and molecular properties of this valuable enzyme such as pH and temperature optima, glucose tolerance, substrate specificity, molecular weight, and multiplicity. Furthermore, it describes molecular cloning and expression of bacterial, fungal and metagenomic β-glucosidases. Finally, it highlights the potential biotechnological applications of β-glucosidases.

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“…Na + had no effect on the activities of lipase sourced from Pseudomonas aeruginosa SRT9 [18] and also lipase sourced from Vibrio fischeri [16]. Ca 2+ slightly increased the activity of lipase from Pseudomonas aeruginosa SRT9 [18].…”

Section: Effect Of Metal Ions and Chelatorsmentioning

confidence: 89%

“…Meanwhile, Rajintha et al reported that Ca 2+ had no effect on lipase from Vibrio fischeria. Fe 2+ , Ag + , Cu 2+ , Hg + , Pb 2+ and Zn 2+ reduced the activity of lipase from a new strain of Pseudomonas aeruginosa SRT9 [16]. Li+, Na + and NH 4+ increased the enzyme's activity slightly whereas Hg+, Zn 2+ , Fe 3+ , Pb 2+ and Al3 + at the high concentration strongly inhibited the activity of lipase from thermophilic Anoxybacillus flavithermus HBB134 [17].…”

Section: Effect Of Metal Ions and Chelatorsmentioning

confidence: 95%

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Microbial Lipases: A Prospect for Biotechnological Industrial Catalysis for Green Products: A Review

Ugo¹,

Amara²,

Cn³

et al. 2017

Ferment Technol

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Microbes have been novel hosts for suitable industrial enzymes including lipases. With the rapid increase in biotechnological industries, there is need for improvement of bioproducts, enhance environmental safety and product yield. Microbes are qualified biological arsenal for the achievement of the above mentioned targets in the industrial sectors. Lipases as versatile biological catalyst has given a promising prospect in meeting the needs for most industries such as biodiesel, foods and drinks, leather, textile, detergents, pharmaceuticals and medicals. Catalytic importance of lipases includes hydrolysis, esterification and transesterification. Each of the mentioned reactions has their industrial applications. Lipases exhibit various properties, with respect to its source. Immobilization has made the use of microbial lipases attain its optimum performance and hence suitable for various reaction and the need to add flavor to the immobilization processes.

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Purification and Characterization of the Lipase from Marine Vibrio fischeri

Cited by 15 publications

References 29 publications

Production and Partial Characterization of Lipase from Pseudomonas putida

Production and Partial Characterization of Lipase from Pseudomonas putida

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

Microbial Lipases: A Prospect for Biotechnological Industrial Catalysis for Green Products: A Review

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