Facile fabrication of a recyclable nanobiocatalyst: immobilization of <i>Burkholderia cepacia</i> lipase on carbon nanofibers for the kinetic resolution of a racemic atenolol intermediate

Soni, Surbhi; Dwivedee, Bharat P.; Banerjee, Uttam Chand

doi:10.1039/c8ra05463k

Cited by 14 publications

(4 citation statements)

References 78 publications

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“…They calculated the kinetic parameters and found that KM was 2.07 mM and VMAX was 1.73 mmol min −1 g −1 for the free lipase. In contrast, the values recorded for immobilized lipase were 0.15 mM and 1.77 mmol min −1 g −1 , respectively [41]. In comparison to the results obtained in our study, the data are analogous since the activated carbon did not alter the VMAX.…”

Section: Kinetics Parameterssupporting

confidence: 77%

“…These results agree with our findings. In addition, two different techniques were employed by Soni et al to immobilize Burkholderia cepacia lipase treated with surface carbon nanofibers, adsorption and covalent immobilization [41]. They calculated the kinetic parameters and found that K M was 2.07 mM and V MAX was 1.73 mmol min −1 g −1 for the free lipase.…”

Section: Kinetics Parametersmentioning

confidence: 99%

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Palm Raceme as a Promising Biomass Precursor for Activated Carbon to Promote Lipase Activity with the Aid of Eutectic Solvents

et al. 2022

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This study concerns the role of activated carbon (AC) from palm raceme as a support material for the enhancement of lipase-catalyzed reactions in an aqueous solution, with deep eutectic solvent (DES) as a co-solvent. The effects of carbonization temperature, impregnation ratio, and carbonization time on lipase activity were studied. The activities of Amano lipase from Burkholderia cepacia (AML) and lipase from the porcine pancreas (PPL) were used to investigate the optimum conditions for AC preparation. The results showed that AC has more interaction with PPL and effectively provides greater enzymatic activity compared with AML. The optimum treatment conditions of AC samples that yield the highest enzymatic activity were 0.5 (NaOH (g)/palm raceme (g)), 150 min, and a carbonization temperature of 400 °C. DES was prepared from alanine/sodium hydroxide and used with AC for the further enhancement of enzymatic activity. Kinetic studies demonstrated that the activity of PPL was enhanced with the immobilization of AC in a DES medium.

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Section: Kinetics Parameterssupporting

confidence: 77%

Section: Kinetics Parametersmentioning

confidence: 99%

Palm Raceme as a Promising Biomass Precursor for Activated Carbon to Promote Lipase Activity with the Aid of Eutectic Solvents

et al. 2022

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“…An immobilized TLL lipase assay was performed using the p -nitrophenyl palmitate ( p -NPP) method ( Soni et al, 2018 ). The substrate solution contained 30 mg of p -NPP in 10 ml of isopropanol.…”

Section: Methodsmentioning

confidence: 99%

Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition

Wang

et al. 2021

Front. Bioeng. Biotechnol.

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The conversion of flavonoid glycosides and their analogs to their lipophilic ester derivatives was developed by nanobiocatalysts from immobilizing Thermomyces lanuginosus lipase (TLL) on polydopamine-functionalized magnetic Fe3O4 nanoparticles (Fe3O4-PDA-TLL). The behavior investigation revealed that Fe3O4-PDA-TLL exhibits a preference for long chain length fatty acids (i.e., C10 to C14) with higher reaction rates of 12.6–13.9 mM/h. Regarding the substrate specificity, Fe3O4-PDA-TLL showed good substrate spectrum and favorably functionalized the primary OH groups, suggesting that the steric hindrances impeded the secondary or phenolic hydroxyl groups of substrates into the bonding site of the active region of TLL to afford the product.

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“…The activity of Fe 3 O 4 @PDA-TLL was determined using the p-nitrophenyl palmitate (p-NPP) method with slight modifications (Soni et al, 2018). An assay reaction mixture containing 0.1 g immobilized enzyme, 0.9 mL Tris-HCl buffer (50 mM, pH 8.0), and 0.1 mL p-NPP solution (a quantity of 30 mg p-NPP was dissolved in 10 mL isopropanol) was incubated at 37 • C for 10 min.…”

Section: Assay Of Fe 3 O 4 @Pda-tll Activitymentioning

confidence: 99%

Highly Efficient Regioselective Decanoylation of Hyperoside Using Nanobiocatalyst of Fe3O4@PDA-Thermomyces lanuginosus Lipase: Insights of Kinetics and Stability Evaluation

Wang

Tian

et al. 2020

Front. Bioeng. Biotechnol.

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The immobilization of Thermomyces lanuginosus lipase on polydopamine-functionalized Fe 3 O 4 magnetic nanoparticles (Fe 3 O 4 @PDA-TLL) as a nanobiocatalyst was successfully performed for the first time, and the Fe 3 O 4 @PDA-TLL was used for regioselective acylation of natural hyperoside with vinyl decanoate. The effects of several crucial factors, such as the reaction solvent, substrate molar ratio, temperature, and immobilized enzyme dosage, were investigated. Under optimum conditions, the reaction rate, 6-regioselectivity, and maximum substrate conversion were as high as 12.6 mM/h, 100%, and 100%, respectively. An operational stability study demonstrated that the immobilized enzyme could maintain 90.1% of its initial maximum conversion even after reusing it five times. In addition, further investigations on the kinetic parameters, like V max , K m , V max /K m , and E a , also revealed that the biocompatible Fe 3 O 4 @PDA could act as an alternative carrier for the immobilization of different enzymes.

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Facile fabrication of a recyclable nanobiocatalyst: immobilization of Burkholderia cepacia lipase on carbon nanofibers for the kinetic resolution of a racemic atenolol intermediate

Abstract: Immobilization of surfactant treated Burkholderia cepacia lipase on the surface of carbon nanofibers was performed via two different methods: adsorption and covalent attachment.

Cited by 14 publications

References 78 publications

Palm Raceme as a Promising Biomass Precursor for Activated Carbon to Promote Lipase Activity with the Aid of Eutectic Solvents

Palm Raceme as a Promising Biomass Precursor for Activated Carbon to Promote Lipase Activity with the Aid of Eutectic Solvents

Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition

Highly Efficient Regioselective Decanoylation of Hyperoside Using Nanobiocatalyst of Fe3O4@PDA-Thermomyces lanuginosus Lipase: Insights of Kinetics and Stability Evaluation

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