Purification and Characterization of Lipase from &lt;i&gt;Aspergillus flavus&lt;/i&gt; PW2961 using Magnetic Nanoparticles.

Kareem, Sarafadeen Olateju; Adebayo, Oluwatobi Samson; Balogun, S. A.; Adeogun, Abideen Idowu; Akinde, S.B

doi:10.4314/njb.v32i1.11

Cited by 10 publications

(8 citation statements)

References 14 publications

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“…It alters the conformation of the active site resulting in a declining substrate-enzyme contact [40]. Like our findings, Thamaraichelvan et al [41] and Kareem et al [42] reported 45 °C as the optimal temperature for A. niger and A. flavus lipases, respectively. The temperatures optimum of P. fellutanum lipase were also coherent with P. verrucosum lipase that exhibited the highest catalytic activity at 42 °C [43].…”

Section: Lipase Activity At Varying Temperatures and Activation Energysupporting

confidence: 80%

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Penicillium fellutanum lipase as a green and ecofriendly biocatalyst for depolymerization of poly (ɛ‐caprolactone): Biochemical, kinetic, and thermodynamic investigations

Amin

Bhatti

Nawaz

et al. 2021

Biotech and App Biochem

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Microbial lipases hold a prominent position in biocatalysis by their capability to mediate reactions in aqueous and nonaqueous media. Herein, a lipase from Penicillium fellutanum was biochemically characterized and investigated its potential to degrade poly (ɛ‐caprolactone) (PCL). The lipase exhibited stability over a broad pH spectrum and performed best at pH 8.5 and 45 °C. The activation energy was determined to be 66.37 kJ/mol by Arrhenius plot, whereas Km and Vmax for pNPP hydrolysis were 0.75 mM and 83.33 μmol/mL/Min, respectively. A rise in temperature reduced the Gibbs free energy, whereas the enthalpy of thermal unfolding (∆H*) remains the same up to 54 °C following a modest decline at 61 °C. The entropy (∆S*) of the enzyme demonstrated an increasing trend up to 54 °C and dropped at 61 °C. Lipase retained stability by incubation with various industrially relevant organic solvents (benzene, hexanol, ether, and acetone). However, exposure to urea and guanidine hydrochloride influenced its catalytic activity to different extents. Under optimal operating conditions, lipase catalyzed the excellent degradation of PCL film degradation leading to 66% weight loss, increased surface erosion, and crystallinity. Fourier‐transform infrared spectrometry, differential scanning calorimetry, and scanning electron microscopy studies monitored the weight loss after enzymatic hydrolysis. The findings indicate that P. fellutanum lipase would be a prospective biocatalytic system for polyesters depolymerization and environmental remediation.

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Section: Lipase Activity At Varying Temperatures and Activation Energysupporting

confidence: 80%

“…[41] and Kareem et al. [42] reported 45 °C as the optimal temperature for A. niger and A. flavus lipases, respectively. The temperatures optimum of P. fellutanum lipase were also coherent with P. verrucosum lipase that exhibited the highest catalytic activity at 42 °C [43].…”

Section: Resultsmentioning

confidence: 99%

Penicillium fellutanum lipase as a green and ecofriendly biocatalyst for depolymerization of poly (ɛ‐caprolactone): Biochemical, kinetic, and thermodynamic investigations

Amin

Bhatti

Nawaz

et al. 2021

Biotech and App Biochem

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“…A further increase in pH beyond 7.5 presented a declining trend in enzyme activity, indicating the neutral character of A. melleus lipase. Kareem et al 33 reported that lipase from A. flavus PW2961 presented activity over a wide pH range (5)(6)(7)(8)(9), with an optimal activity at pH 7.0. Likewise, the optimal activities of lipases produced by two species of Aspergillus performed best at pH 6.0.…”

Section: Resultsmentioning

confidence: 99%

Kinetic and thermodynamic characterization of lipase from Aspergillus melleus and its biocatalytic performance for degradation of poly(ɛ‐caprolactone)

Amin

Bhatti

Bilal

2021

J of Chemical Tech & Biotech

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BACKGROUND: Lipases are an interesting class of enzymes that can be used as biocatalysts for poly(ɛ-caprolactone) degradation. This work reports on the biochemical characterization of a lipase produced through solid-state fermentation by Aspergillus melleus and its application to degrade poly(ɛ-caprolactone).RESULTS: Lipase demonstrated the best activity and remained stable even after 24 h at an optimal pH of 7.5 and 40 °C. The K m and V max values for p-nitrophenyl palmitate hydrolysis derived from Lineweaver-Burk plot were 0.286 mmol L −1 and 142.86 ∼mol mL −1 min −1 , respectively. Thermal inactivation studies revealed a half-life of 1732.5 min (28.88 h) at 40 °C, and dramatically reduced at elevated temperatures. The activation energy for substrate hydrolysis was 28.81 kJ mol −1 , whereas the entropy, enthalpy (ΔH°) and free energy (ΔG°) of thermal inactivation of lipase were determined to be 168.73 J mol −1 K −1 , 160.60 and 107.79 kJ mol −1 , respectively, at 40 °C. Increase in temperature showed a decline in ΔG°, but ΔH* remained constant. Incubation with organic solvents did not influence the enzyme stability; however, urea and guanidine hydrochloride reduced the lipase activity. Under optimal operating conditions, the enzyme presented excellent biocatalytic ability to poly(ɛ-caprolactone) film degradation, leading to 53% weight loss. Characterization techniques, such as Fourier transform infrared, differential scanning calorimetry and scanning electron microscopy, corroborated the effective biodegradation of poly(ɛ-caprolactone).CONCLUSION: In conclusion, broad working pH, marked stability in the presence of organic solvents, and poly(ɛ-caprolactone) degradation constitutes a lipase from A. melleus as a promising candidate for large-scale bioremediation of solid waste.

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“…Lipase from Aspergillus flavus PW2961 was thermostable at temperature 40, 50, and 60°C by retaining 91, 86, and 79% residual activity, respectively, after 4 h incubation [48]. Cold adaptive lipase from Staphylococcus lipolyticus sp.…”

Section: Discussionmentioning

confidence: 99%

“…Purified lipase from Y. lipolytica retained 95 and 83% of its original activity for 4 h at 30 and 35 °C, respectively, but only 32 and 5% of the activity was left when it was incubated for 4 h at 40 and 45 °C, respectively . Lipase from Aspergillus flavus PW2961 was thermostable at temperature 40, 50, and 60 °C by retaining 91, 86, and 79% residual activity, respectively, after 4 h incubation . Cold adaptive lipase from Staphylococcus lipolyticus sp.…”

Section: Discussionmentioning

confidence: 99%

Purification of lipase from Aspergillus fumigatus using Octyl Sepharose column chromatography and its characterization

2018

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Lipases are ubiquitous biological macromolecules which have many industrial and environmental applications. The purpose of this study was to purify lipase from Aspergillus fumigatus by using Octyl Sepharose column chromatography. The enzyme was purified by ammonium sulfate precipitation and hydrophobic interaction chromatography which resulted in sevenfold purification. The molecular weight of protein using Native-PAGE was found to be 70 kDa. The apparent molecular weight by SDS-PAGE was found to be 35 kDa which indicated that the enzyme was homodimer. The optimum temperature and pH for activity of the enzyme was found to be 40 °C and 9.0, respectively. The kinetic parameters V and K of the purified lipase were 10.42 µmol min mg and 9.89 mM, respectively. Detergents Tween-20 and Triton X-100 inhibited enzyme activity. However, there was minimal loss of enzyme activity with SDS and Tween-80. All metal ions inhibited the enzyme activity. Among solvents, maximum loss (65%) in the enzyme activity was in hexane.

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Purification and Characterization of Lipase from <i>Aspergillus flavus</i> PW2961 using Magnetic Nanoparticles.

Cited by 10 publications

References 14 publications

Penicillium fellutanum lipase as a green and ecofriendly biocatalyst for depolymerization of poly (ɛ‐caprolactone): Biochemical, kinetic, and thermodynamic investigations

Penicillium fellutanum lipase as a green and ecofriendly biocatalyst for depolymerization of poly (ɛ‐caprolactone): Biochemical, kinetic, and thermodynamic investigations

Kinetic and thermodynamic characterization of lipase from Aspergillus melleus and its biocatalytic performance for degradation of poly(ɛ‐caprolactone)

Purification of lipase from Aspergillus fumigatus using Octyl Sepharose column chromatography and its characterization

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