Activity and Stability of Lipase Preparations from <i>Penicillium corylophilum</i>: Potential Use in Biocatalysis

Romero, Cintia Mariana; Baigorí, Mario Domingo; Baron, Alessandra Machado; Krieger, Nádia; Pera, Licia María

doi:10.1002/ceat.201300851

Cited by 8 publications

(4 citation statements)

References 21 publications

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“…Besides being stable, the stimulatory effect might be due to decreased flexibility along with favourable structural modification which is necessary for enzyme activity. Similar results were observed in lipase obtained from Penicillium corylophilum with residual activity of 123 and 135% in the presence of ethanol and acetone, respectively (Romero et al 2014). Such solvent stable enzymes have also been obtained from other bacterial strains like P. aeruginosa, Bacillus pumilus, B. cereus BG1 (Gupta and Khare 2009).…”

Section: Effect Of Inhibitors and Solvents On Enzyme Activitysupporting

confidence: 79%

Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media

et al. 2017

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Intravascular thrombosis is one of the major causes of variety of cardiovascular disorders leading to high mortality worldwide. Fibrinolytic enzymes from microbial sources possess ability to dissolve these clots and help to circumvent these problems in more efficient and safer way. In the present study, fibrinolytic protease with higher fibrinolytic activity than plasmin was obtained from Serratia sp. KG-2-1 isolated from garbage dump soil. Response surface methodology was used to study the interactive effect of concentration of maltose, yeast extract + peptone (1:1), incubation time, and pH on enzyme production and biomass. Maximum enzyme production was achieved at 33 °C after 24 h at neutral pH in media containing 1.5% Maltose, 4.0% yeast extract + peptone and other trace elements resulting in 1.82 folds increased production. The enzyme was purified from crude extract using ammonium sulfate precipitation and DEAE-Sephadex chromatography resulting in 12.9 fold purification with 14.9% yield. The purified enzyme belongs to metalloprotease class and had optimal activity in conditions similar to physiological environment with temperature optima of 40 °C and pH optima of 8. The enzyme was found to be stable in various solvents and its activity was enhanced in presence of Na, K, Ba, Cu, Mn, Hg but inhibited by Ca and Fe. Hence, the obtained enzyme may be used as potential therapeutic agent in combating various thrombolytic disorders.

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Section: Effect Of Inhibitors and Solvents On Enzyme Activitysupporting

confidence: 79%

Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media

et al. 2017

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“…However, this species is not recognized as a biocatalyst for biodiesel synthesis. [20]. The research shows that the biocatalyst in this form has a hydrolytic activity of 0.2 U/g of mycelium and shows high stability in organic solvents.…”

Section: Discussionmentioning

confidence: 93%

“…nomius , A . oryzae [11], R. oryzae [19] and Penicillium corylophilum [20]. To date, mycelium-bound lipases from psychrotrophic fungi have not been used in research on the biocatalytic synthesis of biodiesel.…”

Section: Discussionmentioning

confidence: 99%

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Mycelium-bound lipases of psychrophilic and mesophilic fungi as biocatalysts for biodiesel synthesis

Kutyła,

Jaszek,

Jędrys

et al. 2023

Preprint

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In this study, biocatalysts in the form of mycelium-bound lipases of psychrotrophic and mesophilic fungi were screened for their ability to synthesize fatty acid methyl (FAME) and ethyl esters (FAEE). It has been shown that the hydrolytic activity of biocatalysts is not accompanied by their biodiesel synthetic activity. Preliminary studies showed for the first time, that the FTIR technique can be used to predict synthetic activity. The highest correlation between the intensity of the bands and synthetic activity, negative and positive, respectively, was observed for two neighboring bands at 1745 cm-1(R= −0.73) and 1699 cm-1(R= 0.68). The psychrotrophic strainPenicilliumsp. 59, isolated from the soil of the Arctic tundra (Spitsbergen), has been shown for the first time as an efficient whole-cell biocatalyst for fatty acid ethyl ester synthesis and is stable in organic solvents. Mathematical optimization of biosynthesis was also performed using RSM. A molar canola oil conversion value of 83.3% into FAEE was obtained at 24.2 °C in n-hexane using 12.5% of used canola oil and 5.3% of the fungal biocatalyst within 6 h. Dry mycelium ofPenicilliumsp. 59 is a promising new biocatalyst for large-scale biosynthesis of biodiesel, given its low-cost production, high activity at room temperature, no need to mix reactions, and reusability in a minimum of six cycles.

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Production of a fermented solid containing lipases from Penicillium roqueforti ATCC 10110 and its direct employment in organic medium in ethyl oleate synthesis

Soares¹,

Alnoch

Dias

et al. 2021

Biotech and App Biochem

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The production and direct employment in organic medium in the ethyl-oleate synthesis of a fermented solid (FS) containing lipases by Penicillium roqueforti ATCC 10110 (PR10110) was investigated. For the production of this FS, the solidstate fermentation of different agroindustrial waste was used, such as: cocoa shell, sugarcane bagasse, sugarcane bagasse with cocoa shell, and cocoa shell with soybean oil and nutrient solution. The response surface methodology was used to study the effect of independent variables of initial moisture content and inductor concentration, as carbon source and inducer on lipase production. The characterization of the fermented solid in organic medium was also carried out. The highest lipase activity (53 ± 5 U g −1 ) was 16% higher than that obtained with the nonoptimized conditions. The characterization studies observed high stability of the FS in organic solvents for 5 h at 30 • C, as well as at different temperatures, and the residual activity was measured against triolein. The FS was also

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Activity and Stability of Lipase Preparations from Penicillium corylophilum: Potential Use in Biocatalysis

Cited by 8 publications

References 21 publications

Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media

Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media

Mycelium-bound lipases of psychrophilic and mesophilic fungi as biocatalysts for biodiesel synthesis

Production of a fermented solid containing lipases from Penicillium roqueforti ATCC 10110 and its direct employment in organic medium in ethyl oleate synthesis

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