Purification, characterization and application of acidic lipase from Pseudomonas gessardii using beef tallow as a substrate for fats and oil hydrolysis

Ramani, K.; Kennedy, L. John; Ramakrishnan, M.; Sekaran, G.

doi:10.1016/j.procbio.2010.06.023

Cited by 71 publications

(47 citation statements)

References 60 publications

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“…Crude lipase was found active along a wide temperature and pH range and similar range of pH was also reported in a thermo-alkaline Staphylococcus aureus by Bacha et al [33]. Maximum stability and activity in lipase production was also recorded at suboptimal culture (40 °C temperature and 5 pH) conditions which is similar to lipase from Pseudomonas gessardii [34]. According to Ramani et al [34], at this pH and temperature, lipase was suitable for adsorption on the oil-water interface and helpful in the opening of block lid from the active site of the enzyme to lower the activation energy of hydrolysis.…”

Section: Enzyme Activity and Stabilitysupporting

confidence: 80%

Production of Industrially Important Enzymes by Thermobacilli Isolated From Hot Springs of India

Dhyani

Gururani

Selim

et al. 2017

RIB

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Enzymes from thermophilic bacteria have received great attention for their potential applications in various industrial sectors. The present study deals with the production of five thermozymes (amylase, lipase, xylanase, protease and cellulase) from 10 thermophilic bacterial species, originally isolated from two hot springs namely Soldhar and Ringigad in Uttarakhand Himalaya, India. The bacterial isolate GBPI_25 produced maximum amylase (1217.86 U/ml) at 45 °C and 5 pH, GBPI 3 produced maximum lipase (22.59 U/ml) at 65 °C and 9 pH, GBPI_25 produced maximum xylanase (98.07 U/ml) at45 °C and 9 pH, GBPI_35 produced maximum protease (16.66 U/ml) at 55 °C and 9 pH, and GBPI 4 produced maximum cellulose (108.68 U/ml) at 45 °C and 5 pH. Crude enzyme preparations showed thermal and pH activities at broad temperature and pH range between 10-100 °C and 3-11 pH, respectively, with different temperature and pH optima. Amylase, xylanase and cellulase showed maximum activity at 50 °C while lipase and protease showed higher activity at 40 and 60 °C, respectively. Enzyme activity at wide temperature range-cellulase and protease from 10-100 °C, amylase and xylanasefrom10-90 °C, and lipase activity from 10-80 °C were the remarkable records from this study. Similarly, pH range for amylase and lipase activity was recorded from 4-11, for xylanase from 3-9, and for protease and cellulase from 3-10. All the thermozymes showed maximum stability at 40 °C and pH 5 except cellulase that showed higher stability at40 °C and neutral pH.

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Section: Enzyme Activity and Stabilitysupporting

confidence: 80%

Production of Industrially Important Enzymes by Thermobacilli Isolated From Hot Springs of India

Dhyani

Gururani

Selim

et al. 2017

RIB

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“…Lipase-catalyzed esterification, transesterification, and interesterification reactions: an emerging area of green chemistry Lipases are known to carry out hydrolysis of ester bonds in aqueous environments (Liu et al 2008;Ramani et al 2010). Their intrinsic property also permits them to catalyze the reverse reactions of esterification, transesterification, and interesterification in nonaqueous and microaqueous milieu.…”

Section: Applications Of Lipasesmentioning

confidence: 99%

An insight into microbial lipases and their environmental facet

Kanmani¹,

Aravind²,

Kumaresan³

2014

Int. J. Environ. Sci. Technol.

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Lipases are serine hydrolases that catalyze the hydrolysis and synthesis of esters formed from glycerol and long-chain fatty acids, by acting at the oil-water interface. Lipases from microbial sources have received heightened attention for an array of industrial applications, and these enzymes have been well exploited in the environmental sector as well. In this article, we present an overview of microbial lipase, including the microorganisms from which it could be produced; the application of recombinant DNA technology tools to produce lipase with enhanced properties, the effective use of waste materials as substrates for lipase production; the usage of statistical tools to efficiently optimize the production medium; lipase purification strategies; and the immobilization of the enzyme on a variety of support materials. The next section of the article provides a gist of its application in diversified spheres and focusses exclusively on the environmentally relevant ones. Lipasecatalyzed esterification, transesterification, and interesterification reactions, an emerging area of green chemistry; lipase-mediated in vitro biopolymer synthesis and degradation; and the application of lipase for remediating fat and oil constituents in wastewater are dealt with in-depth. When its full potential is harnessed, the enzyme could play a pivotal role in environmental management.

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“…Lipase activity is usually influenced by the pH value of media. In common, lipases from bacteria are active at a wide range of pH value and have neutral or base optimum pH [6,18]. Based on the result exhibited at Fig.…”

Section: Effect Of Various Ph Toward Lipase Activity Figure 2 Effectmentioning

confidence: 97%

Partial purification and biochemical characterization of extracellular lipase from Azospirillum sp. JG3 bacteria

Lestari¹,

Raharjo²,

Matsjeh³

et al. 2016

AIP Conference Proceedings

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Abstract. An extracellular lipase from Azospirillum sp.JG3 bacteria was partially purified by ammonium sulfate fractionation. Production of crude extract lipase in Nutrient Broth medium fortified with 1 % olive oil as inducer, fractionation of lipase using ammonium sulfate, and characterization of the highest specific activity of lipase fraction have been achieved in this study. The ammonium sulfate lipase fraction which has highest specific activity is F60 with its value is 12,283.33 U/mg protein. The optimum lipase activity of F60 was achieved at 40° C and pH 7.0. The addition of 1.0 mM EDTA strongly decreased its activity. It considered that this lipase was a metalloenzyme. The addition of 1.0 mM Ca 2+ solution showed that this metal ion increased lipase activity, it indicated that Ca 2+ ion is an activator of this lipase. Whereas addition of Mg 2+ , Zn 2+ , Co 2+ , and Cu 2+ metal ions decreased its activity. Effect of surfactants and commercial detergents addition towards lipase activity showed that all treatments decreased the activity.

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Purification, characterization and application of acidic lipase from Pseudomonas gessardii using beef tallow as a substrate for fats and oil hydrolysis

Cited by 71 publications

References 60 publications

Production of Industrially Important Enzymes by Thermobacilli Isolated From Hot Springs of India

Production of Industrially Important Enzymes by Thermobacilli Isolated From Hot Springs of India

An insight into microbial lipases and their environmental facet

Partial purification and biochemical characterization of extracellular lipase from Azospirillum sp. JG3 bacteria

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