An extracellular solvent stable alkaline lipase from Pseudomonas sp. DMVR46: Partial purification, characterization and application in non-aqueous environment

Patel, Viraat; Nambiar, Shruti; Madamwar, Datta

doi:10.1016/j.procbio.2014.06.007

Cited by 39 publications

(22 citation statements)

References 37 publications

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“…3a). The obtained results of the present study was in accordance with the findings by Patel et al (2014) who reported that the alkaline lipase originated from Pseudomonas sp. DMVR46 retained 100% of its maximum activity at pH 8.5 after 30 min of incubation.…”

Section: Partial Purification Of Lipasesupporting

confidence: 93%

“…The obtained results of the present study were in accordance with the findings of Emtenani et al (2013), who achieved negative influence of metal ions on the lipase activity of B. subtilis DR8806. On the other hand, Patel et al (2014) acids complexes produced during the catalysis and probable elimination of product inhibition on lipase activity (Patel et al, 2014). The inhibitory effect of the chelating agent (EDTA) on the lipolytic activity of the partially purified enzyme of B. atrophaeus FSHM2 (Table 3) was in agreement with the results by Dandavate et al (2009).…”

Section: Partial Purification Of Lipasesupporting

confidence: 82%

“…For example, Patel et al (2014) isolated an organic solvent-stable Pseudomonas sp. DMVR46 from oil spilling sites near the industrial area able to produce alkaline lipase.…”

Section: Resultsmentioning

confidence: 99%

“…DMVR46 retained 100% of its maximum activity at pH 8.5 after 30 min of incubation. They found 50% decrease in the relative activity following pH alteration to 10 (Patel et al, 2014).…”

Section: Partial Purification Of Lipasementioning

confidence: 99%

“…Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) are a group of serine hydrolases which catalyze the hydrolysis, esterification, transesterification, acidolysis, aminolysis and alcoholysis of triacylglycerols or other water-insoluble esters into diacylglycerols, monoacylglycerols, Free Fatty Acids (FFA) and glycerol (Kumar et al, 2012;Patel et al, 2014). Compared to animal and plant-derived lipases, microbial lipases have received great attention owing to their ability to catalyze a wide variety of reactions in both aqueous and nonaqueous phases and relative cost-effectiveness of their production (Bouaziz et al, 2011;Andualema and Gessesse, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Partial Purification and Characterization of a Thermoalkalophilic Lipase Originated from Bacillus atrophaeus FSHM2 and its Application for Ester Synthesis

Ameri¹,

Shakibaie²,

Amirpour-R³

et al. 2015

Biotechnology

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A B S T R A C T A thermoalkalophilic lipase producing bacterial strain, identified asBacillus atrophaeus FSHM2 using 16S rDNA sequencing analysis was isolated from salty soil and its lipase was partially purified and characterized. The obtained results revealed that glucose, hazelnut oil, urea and calcium ion positively affected the lipase production by increasing the lipolytic activity to 13582.5, 6270, 4442 and 5505 U LG 1 , respectively compared to that of basal medium (4150 U LG 1 ). The partially purified lipase acted optimally at pH 9 and retained 88.2% of its initial activity after 1 h of incubation at 100°C. A two fold increase in the relative activity of the partially purified lipase was obtained in the presence of 4 M of NaCl. Application of the partially purified lipase for the synthesis of ethyl and methyl valerate in the organic solvent medium (xylene) resulted in 81.6 and 62.4% esterification, respectively, after 24 h of incubation.

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Section: Partial Purification Of Lipasesupporting

confidence: 93%

Section: Partial Purification Of Lipasesupporting

confidence: 82%

“…For example, Patel et al (2014) isolated an organic solvent-stable Pseudomonas sp. DMVR46 from oil spilling sites near the industrial area able to produce alkaline lipase.…”

Section: Resultsmentioning

confidence: 99%

“…DMVR46 retained 100% of its maximum activity at pH 8.5 after 30 min of incubation. They found 50% decrease in the relative activity following pH alteration to 10 (Patel et al, 2014).…”

Section: Partial Purification Of Lipasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Partial Purification and Characterization of a Thermoalkalophilic Lipase Originated from Bacillus atrophaeus FSHM2 and its Application for Ester Synthesis

Ameri¹,

Shakibaie²,

Amirpour-R³

et al. 2015

Biotechnology

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Production and application of a thermostable lipase from Serratia marcescens in detergent formulation and biodiesel production

García‐Silvera

Martínez‐Morales

Bertrand

et al. 2017

Biotech and App Biochem

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In this study, extracellular lipase was produced by Serratia marcescens wild type and three mutant strains. The maximum lipase activity (80 U/mL) was obtained with the SMRG4 mutant strain using soybean oil. Using a 2 factorial design, the lipase production increased 1.55-fold (124 U/mL) with 4% and 0.05% of soybean oil and Triton X-100, respectively. The optimum conditions for maximum lipase activity were 50 °C and pH 8. However, the enzyme was active in a broad range of pH (6-10) and temperatures (5-55 °C). This lipase was stable in organic solvents and in the presence of oxidizing agents. The enzyme also proved to be efficient for the removal of triacylglycerol from olive oil in cotton cloth. A Box-Behnken experimental design was used to evaluate the effects of the interactions between total lipase activity, buffer pH, and wash temperatures on oil removal. The model obtained suggested that all selected factors had a significant impact on oil removal, with optimum conditions of 550 U lipase, 45 °C, pH 9.5, with 79.45% removal. Biotransformation of waste frying oil using the enzyme and in presence of methanol resulted in the synthesis of methyl esters such as methyl oleate, methyl palmitate, and methyl stearate.

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Food‐Grade Expression and Characterization of a Dextranase from Chaetomium gracile Suitable for Sugarcane Juice Clarification

Zhao

Wang

Wei

et al. 2020

Chemistry & Biodiversity

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The microbial production of dextranase using cheap carbon sources is beneficial to solve the economic loss caused by the accumulation of dextran in syrup. A food-grade microbial cell factory was constructed by introducing the dextranase encoding gene DEX from Chaetomium gracile to the chromosome of Bacillus subtilis, and the antibiotic resistance marker gene was subsequently deleted via the Cre/loxP strategy. The dual-promoter system with a sequentially arranged constitutive P43 promoter resulted in an 85 % increase in DEX expression. Under the optimal fermentation conditions of 10 g/L maltose, 15 g/L casein, 1 g/L Na 2 HPO 4 , 1 g/L FeSO 4 and 8 g/ L NaCl, DEX activity was increased from 2.625 to 64.34 U/mL. Recombinant DEX was purified 5.98-fold with a recovery ratio of 26.67 % and specific activity of 3935.02 U/mg. Enzyme activity was optimal at 55°C and pH 5.0 and remained 80.34 % and 71.36 % of the initial activity at 55°C and pH 4.0 after 60 min, respectively. The enzyme possessed high activity in the presence of Co 2 + , while Ag + showed the strongest inhibition ability. The optimal substrate was 20 g/L dextran T-2000. The findings could facilitate the low-cost, large-scale production of food-grade DEX for use in the sugar industry.

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An extracellular solvent stable alkaline lipase from Pseudomonas sp. DMVR46: Partial purification, characterization and application in non-aqueous environment

Cited by 39 publications

References 37 publications

Partial Purification and Characterization of a Thermoalkalophilic Lipase Originated from Bacillus atrophaeus FSHM2 and its Application for Ester Synthesis

Partial Purification and Characterization of a Thermoalkalophilic Lipase Originated from Bacillus atrophaeus FSHM2 and its Application for Ester Synthesis

Production and application of a thermostable lipase from Serratia marcescens in detergent formulation and biodiesel production

Food‐Grade Expression and Characterization of a Dextranase from Chaetomium gracile Suitable for Sugarcane Juice Clarification

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