Immobilization of laccase on modified Fe3O4@SiO2@Kit-6 magnetite nanoparticles for enhanced delignification of olive pomace bio-waste

Amin, Ruhul; Khorshidi, Alireza; Shojaei, Abdollah Fallah; Rezaei, Shahla; Faramarzi, Mohammad Ali

doi:10.1016/j.ijbiomac.2018.03.086

Cited by 70 publications

(26 citation statements)

References 50 publications

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“…The raising of the optimum reactive temperature and pH could be explained by the fact that covalent binding between enzyme and NFM would change the enzyme's microenvironment and protect it from conformational denaturation. 40,41 Moreover, the stability of laccase was significantly improved after laccase immobilization, as its reactivity remained almost unchanged over a temperature range of 30-60°C and over a pH range of 5-8. These results confirmed that immobilization of the enzyme onto NFM could significantly improve enzyme stability, which would allow its application in wider processing scenarios.…”

Section: Morphology Of Carriers After Laccase Immobilizationmentioning

confidence: 99%

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: Morphology Of Carriers After Laccase Immobilizationmentioning

confidence: 99%

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

et al. 2020

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“…However, the industrial applications of laccase are still seriously limited owing to their poor stability and high cost [7]. It is well known that these limitations can be overcome by immobilization technology [8][9][10][11][12]. In earlier studies, Rogalski et al immobilized laccase on controlled porosity glass and measured its activity in the aqueous solution containing organic solvents [13].…”

Section: Introductionmentioning

confidence: 99%

An Improved Method to Encapsulate Laccase from Trametes versicolor with Enhanced Stability and Catalytic Activity

Zhang

Chen

et al. 2018

Catalysts

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In this work, laccase from Trametes versicolor pretreated with copper ion solution was entrapped in copper alginate beads. The presence of laccase in copper alginate beads was verified by Fourier transform infrared (FTIR) spectroscopy. The alginate concentration used was optimized based on the specific activity and immobilization yield. After entrapment, laccase presents perfect pH stability and thermal stability with 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) as the substrate. Moreover, laccase in copper alginate beads exhibits good reusability during continuous batch operation for removing 2,4-dichlorophenol. More importantly, owing to the coupled effect of copper ion activation and copper alginate entrapment, the entrapped laccase shows a 3.0-fold and a 2.4-fold increase in specific activity and 2,4-DCP degradation rate compared with that of free laccase, respectively.

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“…Immobilization of celluclast 1.5L and BGL was more efficient compared to that of previous reports using a styrene/maleic anhydride copolymer, and amine‐modified magnetic and silica nanoparticles . Similarly, the laccase immobilized on APTES‐GLA‐modified Fe 3 O 4 particles was more effective than the previously immobilized laccase on Fe 3 O 4 @SiO 2 @KIT‐6 composite magnetite particles …”

Section: Discussionmentioning

confidence: 57%

Enhanced Saccharification and Fermentation of Rice Straw by Reducing the Concentration of Phenolic Compounds Using an Immobilized Enzyme Cocktail

Kumar

Patel

Gupta

et al. 2019

Biotechnology Journal

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The production of bioethanol from rice straw can contribute to the rural economy and provide clean fuel in a sustainable manner. However, phenolic compounds, which are mostly produced during acid pretreatment of biomass, act as inhibitors of fermenting microorganisms. Laccase is well known for its ability to oxidize lignin and phenolic compounds derived from lignocellulosic biomass. In the present study, an immobilized enzyme cocktail containing laccase was isevaluated in regard to its ability to enhance the saccharification and fermentation processes by reducing the amount of phenolic compounds produced. Saccharification of rice straw with the laccase‐supplemented immobilized enzyme cocktail reduced phenolic compounds by 73.8%, resulting in a saccharification yield of 84.6%. In addition, improved yeast performance was is noted during the fermentation process, resulting in a 78.3% conversion of sugar into ethanol with an ethanol productivity of 0.478 g/L/h. To the best of our knowledge, this is the first description of the use of an immobilized enzyme cocktail comprised of Celluclast 1.5L, β‐glucosidase, and laccase for the production of bioethanol from rice straw. This study details a potential approach to producing biofuels from agricultural biomass, the applicability of which can be improved through up‐scaling.

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Immobilization of laccase on modified Fe3O4@SiO2@Kit-6 magnetite nanoparticles for enhanced delignification of olive pomace bio-waste

Cited by 70 publications

References 50 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

An Improved Method to Encapsulate Laccase from Trametes versicolor with Enhanced Stability and Catalytic Activity

Enhanced Saccharification and Fermentation of Rice Straw by Reducing the Concentration of Phenolic Compounds Using an Immobilized Enzyme Cocktail

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