Monoolein production by triglycerides hydrolysis using immobilized Rhizopus oryzae lipase

Ghattas, Nesrine; Abidi, Ferid; Galai, Said; Marzouki, M. Néjib; Salah, Abderraouf Ben

doi:10.1016/j.ijbiomac.2014.04.017

Cited by 15 publications

(7 citation statements)

References 46 publications

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“…Another search found that laccase immobilized in calcium alginate beads retained about 70% activity after seven cycles were used . The decrease in laccase activity with more reaction cycles might be due to the conformational changes caused by repeated use, during which enzyme inactivation, the blocking of some reaction products, the loss of nanofiber and removal of enzyme from membrane during washing may occur …”

Section: Resultsmentioning

confidence: 99%

“…47 The decrease in laccase activity with more reaction cycles might be due to the conformational changes caused by repeated use, during which enzyme inactivation, the blocking of some reaction products, the loss of nanofiber and removal of enzyme from membrane during washing may occur. 48 Oxidation of ginkgolic acid in G. biloba leaf extract The ability of NFM-immobilized laccase to degrade C13, C15, and C17 ginkgolic acid through oxidation was examined using C13, C15, and C17 ginkgolic acid as targeted compounds. After incubating with the laccase immobilized system, the amount of C13, C15, and C17 ginkgo acid significantly reduced as clearly indicated by the HPLC chromatogram.…”

Section: Determination Of Kinetic Parameters For Laccase Immobilized mentioning

confidence: 99%

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Enzymatic degradation of ginkgolic acid by laccase immobilized on novel electrospun nanofiber mat

et al. 2020

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BACKGROUND Ginkgo biloba leaf extract contains many active ingredients that are beneficial for health. However, ginkgolic acid, one of the major components found in G. biloba extract, may cause serious allergic and toxic side effects. The purpose of this study is to immobilize the laccase system on the electrospun nylon fiber mat (NFM) to hydrolyze the ginkgolic acid in G. biloba leaf extract efficiently. RESULTS Novel electrospinning technology successfully produced high‐quality nanoscopic fiber mats made of a mixture of multi‐walled carbon nanotube and nylon 6,6. Laccase that was immobilized onto the NFM exhibited much higher efficiency in the catalyzation of 2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulfonic acid) diammonium salt (ABTS) than nylon 6,6 pellets. After being immobilized onto the NFM, the pH and temperature stability of laccase were significantly improved. The NFM‐immobilized laccase could maintain more than 50% of its original activity even after 40 days of storage or 10 operational cycles. The kinetic parameters, including rate constant (K), the time (τ50) in which 50% of ginkgolic acid hydrolysis was reached, the time (τcomplete) required to achieve complete ginkgolic acid hydrolysis, Km and Vmax were determined, and were 0.07 ± 0.01 min−1, 8.97 ± 0.55 min, 45.45 ± 2.79 min, 0.51 ± 0.09 mM and 0.49 ± 0.03 mM min−1 mg−1, respectively. CONCLUSION The result successfully demonstrated the strong potential of using novel electrospun nanofiber mats as enzyme immobilization platforms, which could significantly enhance enzyme activity and stability. © 2020 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 99%

Section: Determination Of Kinetic Parameters For Laccase Immobilized mentioning

confidence: 99%

Enzymatic degradation of ginkgolic acid by laccase immobilized on novel electrospun nanofiber mat

et al. 2020

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“…But it may not be strong enough and the enzymes probably fall off during washing and operation [ 30 ]. Entrapment method is trapped enzyme in insoluble beads or microspheres but this insoluble carrier may block the substrates in and the product out [ 31 ]. Cross-linkage method is to covalently bond enzymes together to create aggregates.…”

Section: Introductionmentioning

confidence: 99%

Immobilization ofYarrowia lipolyticaLipase on Macroporous Resin Using Different Methods: Characterization of the Biocatalysts in Hydrolysis Reaction

Sun

Sheng

Sun

2015

BioMed Research International

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To improve the reusability and organic solvent tolerance of microbial lipase and expand the application of lipase (hydrolysis, esterification, and transesterification), we immobilized marine microbial lipase using different methods and determined the properties of immobilized lipases. Considering the activity and cost of immobilized lipase, the concentration of lipase was fixed at 2 mg/mL. The optimal temperature of immobilized lipases was 40°C and 5°C higher than free lipase. The activities of immobilized lipases were much higher than free lipase at alkaline pH (more than 50% at pH 12). The free lipase lost most activity (35.3%) and immobilized lipases retained more than 46.4% of their initial activity after 3 h heat treatment at 70°C. At alkaline pH, immobilized lipases were more stable than free lipase (more than 60% residue activity at pH 11 for 3 h). Immobilized lipases retained 80% of their activity after 5 cycles and increased enzyme activity (more than 108.7%) after 3 h treatment in tert-butanol. Immobilization of lipase which improved reusability of lipase and provided a chance to expand the application of marine microbial lipase in organic system expanded the application range of lipase to catalyze hydrolysis and esterification in harsh condition.

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“…When RoL was immobilized in alginate gel beads, the pH shifted from pH 8 to 7. The reason of the shifting was due to surface and residual charges on the support, for example polycationic support would result in acidic shift while polyanionic support caused in a shift to more basic pH values [23]. Therefore, immobilized enzymes are mostly active at broader pH compared to free enzymes.…”

Section: Characterization Of Rol Immobilized On Polypropylene Supportmentioning

confidence: 99%

Enhanced Performance of Immobilized Rhizopus oryzae Lipase on Coated Porous Polypropylene Support with Additives

et al. 2021

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The immobilization of Rhizopus oryzae lipase (RoL) by hydrophobic adsorption on polypropylene supports with additives was investigated. Additives such as hen egg albumin, sodium caseinate and CAVAMAX® W6 were used to coat the support during immobilization where the immobilized RoL on coated support was compared to those of noncoated support. Following the immobilization, the catalytic activity of immobilized RoL was characterized based on different temperatures and pH. The immobilized RoL without additives showed optimal lipase activity at an optimum temperature of 50 °C and pH 6. However, RoL lipase that was immobilized on support treated with CAVAMAX® W6 had better performance in terms of hydrolytic activity and stability as compared to other additives. In addition, by having a support treated with hen egg albumin, the immobilized RoL was capable of yielding higher ester during esterification reactions.

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Monoolein production by triglycerides hydrolysis using immobilized Rhizopus oryzae lipase

Cited by 15 publications

References 46 publications

Enzymatic degradation of ginkgolic acid by laccase immobilized on novel electrospun nanofiber mat

Enzymatic degradation of ginkgolic acid by laccase immobilized on novel electrospun nanofiber mat

Immobilization ofYarrowia lipolyticaLipase on Macroporous Resin Using Different Methods: Characterization of the Biocatalysts in Hydrolysis Reaction

Enhanced Performance of Immobilized Rhizopus oryzae Lipase on Coated Porous Polypropylene Support with Additives

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