Immobilization of Rhus vernicifera laccase on sepiolite; effect of chitosan and copper modification on laccase adsorption and activity

Olshansky, Yaniv; Masaphy, Segula; Root, Robert; Rytwo, Giora

doi:10.1016/j.clay.2017.11.006

Cited by 23 publications

(11 citation statements)

References 25 publications

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“…In contrast, fungal laccases show higher redox potential between 470 and 810 [35]. Laccase immobilization on various kinds of supports has been established, including silica [24], kaolinites [10], membranes [36], and sepiolite [37]. Although numerous kinds of supports have been used to immobilize laccase, still there is a need for efficient supports to retain high loading, improved stability, and reusability for a potential application.…”

Section: Introductionmentioning

confidence: 99%

“…Laccase from Trametes versicolor has been largely studied for immobilization [10,24,38]. A few reports have been noted for immobilization of R. vernicifera laccase (RvLac) on supports, including chitosan [26,39], nylon membrane [16], sepiolite [37], and zirconium chloride [28]. In this study, RvLac immobilization on magnetic nanoparticles Fe 2 O 3 , and Fe 3 O 4 functionally activated by 3-aminopropyltriethoxysilane (APTES) followed with glutaraldehyde was evaluated to improve loading and enzyme properties.…”

Section: Introductionmentioning

confidence: 99%

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Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in Bisphenol A Degradation

et al. 2020

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In the present study, Rhus vernicifera laccase (RvLac) was immobilized through covalent methods on the magnetic nanoparticles. Fe 2 O 3 and Fe 3 O 4 nanoparticles activated by 3-aminopropyltriethoxysilane followed with glutaraldehyde showed maximum immobilization yields and relative activity up to 81.4 and 84.3% at optimum incubation and pH of 18 h and 5.8, respectively. The maximum RvLac loading of 156 mg/g of support was recorded on Fe 2 O 3 nanoparticles. A higher optimum pH and temperature of 4.0 and 45 °C were noted for immobilized enzyme compared to values of 3.5 and 40 °C for free form, respectively. Immobilized RvLac exhibited better relative activity profiles at various pH and temperature ranges. The immobilized enzyme showed up to 16-fold improvement in the thermal stability, when incubated at 60 °C, and retained up to 82.9% of residual activity after ten cycles of reuses. Immobilized RvLac exhibited up to 1.9-fold higher bisphenol A degradation efficiency potential over free enzyme. Previous reports have demonstrated the immobilization of RvLac on nonmagnetic supports. This study has demonstrated that immobilization of RvLac on magnetic nanoparticles is very efficient especially for achieving high loading, better pH and temperature profiles, and thermal-and solvents-stability, high reusability, and higher degradation of bisphenol A.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in Bisphenol A Degradation

et al. 2020

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“…As can be seen in Figure 1 a, the recovery of enzyme activity at this time reached 7.4% when the concentration of genipin in the system was 0. The activity was due to the physical adsorption and ion exchange [ 45 , 46 , 47 ] of chitosan on tannase, which was not easily eluted by the buffer. Enzyme activity recovery and specific enzyme activity were 19.2% and 10.0 U/g, respectively, when the amount of genipin was increased to 0.4 mg/mL.…”

Section: Resultsmentioning

confidence: 99%

Chitosan Activated with Genipin: A Nontoxic Natural Carrier for Tannase Immobilization and Its Application in Enhancing Biological Activities of Tea Extract

et al. 2021

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In this work, a non-toxic chitosan-based carrier was constructed via genipin activation and applied for the immobilization of tannase. The immobilization carriers and immobilized tannase were characterized using Fourier transform infrared spectroscopy and thermogravimetric analysis. Activation conditions (genipin concentration, activation temperature, activation pH and activation time) and immobilizations conditions (enzyme amount, immobilization time, immobilization temperature, immobilization pH, and shaking speed) were optimized. The activity and activity recovery rate of the immobilized tannase prepared using optimal activation and immobilization conditions reached 29.2 U/g and 53.6%, respectively. The immobilized tannase exhibited better environmental adaptability and stability. The immobilized tannase retained 20.1% of the initial activity after 12 cycles and retained 81.12% of residual activity after 30 days storage. The catechins composition analysis of tea extract indicated that the concentration of non-ester-type catechins, EGC and EC, were increased by 1758% and 807% after enzymatic treatment. Biological activity studies of tea extract revealed that tea extract treated with the immobilized tannase possessed higher antioxidant activity, higher inhibitory effect on α-amylase, and lower inhibitory effect on α-glucosidase. Our results demonstrate that chitosan activated with genipin could be an effective non-toxic carrier for tannase immobilization and enhancing biological activities of tea extract.

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“…Wen et al (2019) immobilized laccase in bentonite-derived mesoporous materials and observed a 64% loss of activity after the 5th cycle of use, indicating leaching of the enzyme in the washing steps. Recently, laccases have been successfully immobilized by adsorption on sepiolite modified with chitosan (Olshansky et al 2018), on magnetic iron powder coated with chitosan (Patel et al 2016), on cellulose modified with calcium nano carbonate (Li et al 2018a), on magnetically modified bacterial cellulose (Drozd et al 2018) and other supports. Among inorganic supports, laccases have been immobilized on hybrids of Zirconia-Silica and Zirconia-Silica with copper addition (Jankowska et al 2019), on mesostructured silica (Zdarta et al 2020a), on aluminum oxide (Kołodziejczak-Radzimska et al 2020) and on mesoporous carbon nanospheres (Shao et al 2019).…”

Section: Laccase Immobilization: a Sustainable Strategymentioning

confidence: 99%

Laccases as green and versatile biocatalysts: from lab to enzyme market—an overview

Brugnari

Braga

Santos

et al. 2021

Bioresour. Bioprocess.

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Laccases are multi-copper oxidase enzymes that catalyze the oxidation of different compounds (phenolics and non-phenolics). The scientific literature on laccases is quite extensive, including many basic and applied research about the structure, functions, mechanism of action and a variety of biotechnological applications of these versatile enzymes. Laccases can be used in various industries/sectors, from the environmental field to the cosmetics industry, including food processing and the textile industry (dyes biodegradation and synthesis). Known as eco-friendly or green enzymes, the application of laccases in biocatalytic processes represents a promising sustainable alternative to conventional methods. Due to the advantages granted by enzyme immobilization, publications on immobilized laccases increased substantially in recent years. Many patents related to the use of laccases are available, however, the real industrial or environmental use of laccases is still challenged by cost–benefit, especially concerning the feasibility of producing this enzyme on a large scale. Although this is a compelling point and the enzyme market is heated, articles on the production and application of laccases usually neglect the economic assessment of the processes. In this review, we present a description of laccases structure and mechanisms of action including the different sources (fungi, bacteria, and plants) for laccases production and tools for laccases evolution and prediction of potential substrates. In addition, we both compare approaches for scaling-up processes with an emphasis on cost reduction and productivity and critically review several immobilization methods for laccases. Following the critical view on production and immobilization, we provide a set of applications for free and immobilized laccases based on articles published within the last five years and patents which may guide future strategies for laccase use and commercialization.

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Immobilization of Rhus vernicifera laccase on sepiolite; effect of chitosan and copper modification on laccase adsorption and activity

Abstract: vernicifera laccase on sepiolite; effect of chitosan and copper modification on laccase adsorption and activity, Applied Clay Science, 152, pp 143-147,

Cited by 23 publications

References 25 publications

Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in Bisphenol A Degradation

Rhus vernicifera Laccase Immobilization on Magnetic Nanoparticles to Improve Stability and Its Potential Application in Bisphenol A Degradation

Chitosan Activated with Genipin: A Nontoxic Natural Carrier for Tannase Immobilization and Its Application in Enhancing Biological Activities of Tea Extract

Laccases as green and versatile biocatalysts: from lab to enzyme market—an overview

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