Laccase catalyzed elimination of morphine from aqueous systems

Huber, Daniela; Bleymaier, Klaus; Pellis, Alessandro; Vielnascher, Robert; Daxbacher, Andreas; Greimel, Katrin Julia; Guebitz, Georg M.

doi:10.1016/j.nbt.2018.01.003

Cited by 19 publications

(10 citation statements)

References 42 publications

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“…In recent years, Pellis et al prepared the immobilized laccase using Accurel MP1000 beads as a carrier to facilitate the oxidation of Kraft lignin (KL) and lignosulfonate (LS) [16]. Greimel et al used immobilized laccase to remove morphine and complete morphine elimination was achieved within 30 min [17].…”

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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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 that sense, one of the applications of laccase is the detection of various compounds in certain foods. However, it is also used for the synthesis of chemical compounds, their detection and recently it has been reported that the enzyme is capable of removing morphine from aqueous systems (Huber et al, 2018). This reflects the great potential of the enzyme not only in the food industry but also for the recovery of contaminated areas, hence the importance and relevance of the information presented here.…”

Section: Potential Trends and Current Challengesmentioning

confidence: 62%

Laccases in Food Industry: Bioprocessing, Potential Industrial and Biotechnological Applications

Mayolo‐Deloisa

González‐González

Rito‐Palomares

2020

Front. Bioeng. Biotechnol.

138

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Laccase is a multi-copper oxidase that catalyzes the oxidation of one electron of a wide range of phenolic compounds. The enzyme is considered eco-friendly because it requires molecular oxygen as co-substrate for the catalysis and it yields water as the sole by-product. Laccase is commonly produced by fungi but also by some bacteria, insects and plants. Due it is capable of using a wide variety of phenolic and nonphenolic substrates, laccase has potential applications in the food, pharmaceutical and environmental industries; in addition, it has been used since many years in the bleaching of paper pulp. Fungal laccases are mainly extracellular enzyme that can be recovered from the residual compost of industrial production of edible mushrooms as Agaricus bisporus and Pleurotus ostreatus. It has also been isolated from microorganisms present in wastewater. The great potential of laccase lies in its ability to oxidize lignin, one component of lignocellulosic materials, this feature can be widely exploited on the pretreatment for agro-food wastes valorization. Laccase is one of the enzymes that fits very well in the circular economy concept, this concept has more benefits over linear economy; based on "reduce-reuse-recycle" theory. Currently, biorefinery processes are booming due to the need to generate clean biofuels that do not come from oil. In that sense, laccase is capable of degrading lignocellulosic materials that serve as raw material in these processes, so the enzyme's potential is evident. This review will critically describe the production sources of laccase as by-product from food industry, bioprocessing of food industry by-products using laccase, and its application in food industry.

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“…Each of the dried LS samples was resuspended in ultrapure water at 20 wt % and left for stirring at 40 °C until completely solubilized, followed with a NaOH addition to reach pH 7 (pH at which MtL shows the highest catalytic activity). 11 Enzymatic oxidation was carried out in 500 mL transparent durum bottles with tight-fitting tube holes on the lid to allow the air supply. The reaction was started by introducing 233 nkat/mL laccase and was continuously supplied with 10 cm 3 /min oxygen at 37.5 °C while mixing under vigorous stirring at 900 rpm.…”

Section: Materials and Methodsmentioning

confidence: 99%

Role of Surface Enhancement in the Enzymatic Cross-Linking of Lignosulfonate Using Alternative Downstream Techniques

et al. 2022

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Lignosulfonate (LS), one of the byproducts of the paper and pulp industry, was mainly used as an energy source in the last decade until the valorization of lignin through different functionalization methods grew in importance. Polymerization using multicopper oxidase laccase (from the Myceliophthora thermophila fungus) is one of such methods, which not only enhances properties such as hydrophobicity, flame retardancy, and bonding properties but can also be used for food and possesses pharmaceutical-like antimicrobial properties and aesthetic features of materials. Appropriate downstream processing methods are needed to produce solids that allow the preservation of particle morphology, a vital factor for the valorization process. In this work, an optimization of the enzymatic polymerization via spray-drying of LS was investigated. The response surface methodology was used to optimize the drying process, reduce the polymerization time, and maximize the dried mass yield. Particles formed showed a concave morphology and enhanced solubility while the temperature sensitivity of spray-drying protected the phenol functionalities beneficial for polymerization. Using the optimized parameters, a yield of 65% in a polymerization time of only 13 min was obtained. The experimental values were found to be in agreement with the predicted values of the factors ( R 2 : 95.2% and p -value: 0.0001), indicating the suitability of the model in predicting polymerization time and yield of the spray-drying process.

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Laccase catalyzed elimination of morphine from aqueous systems

Cited by 19 publications

References 42 publications

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

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

Laccases in Food Industry: Bioprocessing, Potential Industrial and Biotechnological Applications

Role of Surface Enhancement in the Enzymatic Cross-Linking of Lignosulfonate Using Alternative Downstream Techniques

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