Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010

Zhao, Lili; Xu, Jian‐He; Zhao, Jian; Pan, Jiang; Wang, Zhilong

doi:10.1016/j.procbio.2008.01.023

Cited by 90 publications

(49 citation statements)

References 36 publications

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“…Estos resultados coinciden con el comportamiento de una lipasa recombinante de Serratia marcescens expresada en Escherichia coli [17] y de Serratia marcescens ECU1010 [18]. la temperatura óptima de crecimiento del microorganismo CCEI-1 para la síntesis de la enzima lipasa y la hidrólisis del aceite de oliva en las condiciones de ensayo fue 30°C.…”

Section: Efecto Del Ph Y La Temperatura Sobre La Producción Enzimáticaunclassified

“…Existen reportes de la estabilidad térmica en la lipasa extracelular de S. marcescens a 50°C [19], las lipasas mG1 y sG1 de S. marcescens expresadas en la levadura Kluyveromyces lactis mostraron actividades relativas de 60 y 29% respectivamente, a 45°C durante 30 minutos [20], mientras que la lipasa CCEI-1l, del presente estudio, tuvo una mayor actividad relativa considerando la temperatura y tiempo de incubación (50°C por 1 hora). la lipasa ECU1010 retuvo el 71% de estabilidad a 50°C durante una hora [18].…”

Section: Evaluación De La Estabilidad Térmica Y Efectos Del Ph En La unclassified

“…En el precipitado enzimático de S. marcescens CCEI-1 se detectaron varias bandas de posibles proteínas alrededor de los 66 kDa, confirmando la presencia de una lipasa microbiana pues existen varios reportes que indican que esta enzima sintetizada por S. marcescens tiene pesos moleculares en este rango, 66,2 kDa [18,20], 65k Da [17,19] y 52 kDa [17].…”

Section: Purificación Parcial De La Enzima Y Electroforesis En Gelunclassified

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INFLUENCIA DE MICROORGANISMOS EN LA DISPONIBILIDAD DE FÓSFORO EN PLÁNTULAS DE CAFÉ (Coffea arabica)

Cisneros¹,

Franco²,

Fernandez³

et al. 2017

BSAA

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Section: Efecto Del Ph Y La Temperatura Sobre La Producción Enzimáticaunclassified

Section: Evaluación De La Estabilidad Térmica Y Efectos Del Ph En La unclassified

Section: Purificación Parcial De La Enzima Y Electroforesis En Gelunclassified

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INFLUENCIA DE MICROORGANISMOS EN LA DISPONIBILIDAD DE FÓSFORO EN PLÁNTULAS DE CAFÉ (Coffea arabica)

Cisneros¹,

Franco²,

Fernandez³

et al. 2017

BSAA

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“…This can be achieved by manipulating growth conditions to optimal level that generally improves the lipase productivity as evidenced in earlier studies (Gupta et al, 2007;Treichel et al, 2010;Rabbani et al, 2013). The most important parameters that critically affect the lipase production are carbon and nitrogen sources (Kumari et al, 2009;Zhao et al, 2008). However, optimization of other nutritional and growth parameters affecting lipase production will be the added advantage for improvement studies.…”

Section: Introductionmentioning

confidence: 99%

Optimization of Lipase Production by Thermo-Alkalophilic Bacillus sp. 8C

Bhosale¹,

Uzma²,

Bismile³

2015

Research J. of Microbiology

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Microbial lipases catalyzing the hydrolysis and synthesis of esters from glycerol and fatty acids are commercially important in food, dairy, detergent and leather industries. In the present study, 15 thermo-alkalophilic bacterial strains isolated from a compost soil sample were screened for lipase production in beef extract nitrate medium containing 1% tributyrin. The strain 8C, giving maximum lipolytic activity was morphologically and biochemically identified as Bacillus sp. Lipase production from strain 8C was optimized by studying effects of incubation period, initial pH of medium, carbon and nitrogen sources, metals, substrates and thiols under static conditions. Lipase production was maximum after 7 days of incubation at 50°C and pH 9.0 and when sesame oil was used as a substrate. Supplementation of ribose or raffinose and ammonium sulphate (1%) as sole sources of carbon and nitrogen also stimulated lipase production over control. Of the different thiols tested, methionine greatly increased lipase production (175 Eu mLG 1 ) whereas, FeCl 3 (50 mM) found to be most suitable metal salt for optimal lipase production (300 Eu mLG 1 ). Under optimized conditions, lipase production by thermo-alkalophilic Bacillus sp. 8C was increased by 6.36 fold compared to unoptimized conditions. Key words: Thermophilic, alkaline, ribose, FeCl 3 , methionine, sesame oil INTRODUCTIONLipases (triglycerol hydrolases (EC 3.1.1.3) are the hydrolytic enzymes belonging to serine hydrolase family and catalyze conversion and synthesis of esters from glycerol and fatty acids. Lipolytic reactions are highly chemo-, regio and or enantioselective and operate at the interface of oil and water (Nguyen et al., 2010). High quality and low energy consumption of lipase catalyzed reactions make them superior over conventional steam splitting methods operating at high temperature and pressure (Treichel et al., 2010). These characteristics of lipases increased their demand in different industries including food and dairy, detergent, cosmetics, leather, paper and pulp, biodiesel and pharmaceutical (Hasan et al., 2007).Thermophilic lipases are of special interest for industrial applications due to their stability and high activity at higher temperatures and being stable in presence of chemicals (Messias et al., 2009;Uttatree et al., 2010). Lipases being third largest selling group of enzymes with more than 1000 t of annual production and approaching to a billion dollar business. Lipases active at alkaline pH are of great importance in detergent industry where these enzymes are used for removal of fat stains and dirt (Bora and Bora, 2012). The use of alkaline lipases in detergent formulation substantially

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“…Gum arabic has been systematically used in in vitro measurements of lipase activity when using long-chain triacylglycerols as substrate (e.g. Zhao et al, 2008). It has generally been assumed that the gum arabic is simply an emulsifying agent stabilizing standard emulsions without interfering with the lipase assay itself.…”

Section: Hydrolysis Of Triacylglycerolsmentioning

confidence: 99%

Differences in hydrolytic abilities of two crude lipases from Geotrichum candidum 4013

Brabcová

Zarevúcká

Macková

2010

Yeast

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The fungus Geotrichum candidum 4013 produces two types of lipases (extracellular and cell-bound). Both enzymes were tested for their hydrolytic ability to pnitrophenyl esters and compounds having a structure similar to the original substrate (triacylglycerols). Higher lipolytic activity of extracellular lipase was observed when triacylglycerols of medium-(C12) and long-(C18) chain fatty acids were used as substrates. Cell-bound lipase preferentially hydrolysed trimyristate (C14). The differences in the abilities of these two enzymes to hydrolyse p-nitrophenyl esters were observed as well. The order of extracellular lipase hydrolysis relation velocity was as follows: p-nitrophenyl decanoate > p-nitrophenyl caprylate > p-nitrophenyl laurate > p-nitrophenyl palmitate > p-nitrophenyl stearate. The cell-bound lipase indicates preference for p-nitrophenyl palmitate. The most striking differences in the ratios between the activity of both lipases (extracellular : cell-bound) towards different fatty acid methyl esters were 2.2 towards methyl hexanoate and 0.46 towards methyl stearate (C18). The Michaelis constant (K m ) and maximum reaction rate (V max ) for p-nitrophenyl palmitate hydrolysis of cell-bound lipase were significantly higher (K m 2.462 mM and V max 0.210 U/g/min) than those of extracellular lipase (K m 0.406 mM and V max 0.006 U/g/min).

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Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010

Cited by 90 publications

References 36 publications

INFLUENCIA DE MICROORGANISMOS EN LA DISPONIBILIDAD DE FÓSFORO EN PLÁNTULAS DE CAFÉ (Coffea arabica)

INFLUENCIA DE MICROORGANISMOS EN LA DISPONIBILIDAD DE FÓSFORO EN PLÁNTULAS DE CAFÉ (Coffea arabica)

Optimization of Lipase Production by Thermo-Alkalophilic Bacillus sp. 8C

Differences in hydrolytic abilities of two crude lipases from Geotrichum candidum 4013

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