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Journal ArticleDOI

Recent developments in the use of tyrosinase and laccase in environmental applications

22 Mar 2017-Critical Reviews in Biotechnology (Taylor & Francis)-Vol. 37, Iss: 7, pp 819-832
TL;DR: This review addressed the disparity in the molecular features and catalytic mechanism of tyrosinases relevant in environmental applications and a perspective on the future use of laccases and tyros in bioremediation was discussed.
Abstract: Our current global environmental challenges include the reduction of harmful chemicals and their derivatives. Bioremediation has been a key strategy to control the massive presence of chemicals in the environment. Enzymes including the phenoloxidases, laccases and tyrosinases, are increasingly being investigated as “green products” in the removal of many chemical contaminants in waters and soils. Both phenoloxidases are widespread in nature and attractive biocatalysts due to their ability to use readily available molecular oxygen as sole cofactor for their catalytic elimination of a large number of chemicals. Taking advantage of their catalytic potentials, remarkable advances have been made in the engineering of laccases to produce suitable biocatalysts in environmental applications. Studies about novel strategies of laccase immobilization and insolubilization for the treatment of chemical contaminants were provided. Likewise, tyrosinases are gaining increasing interest in environmental applicatio...
Citations
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Journal ArticleDOI
TL;DR: This review focuses on some recent novel techniques in preparing co-immobilized multienzymatic systems and the up-to-date advances in the application of multistep synthetic methods.

245 citations

Journal ArticleDOI
TL;DR: This review summarizes the most significant recent advances in the use of laccases and their future perspectives in environmental biotechnology.

209 citations

Journal ArticleDOI
TL;DR: This review summarizes the current state of knowledge regarding the materials used for enzyme immobilization of these oxidoreductase enzymes for environmental applications and provides an improved foundation on which new technological advancements can be made to achieve efficient enzyme-assisted bioremediation.

195 citations

Journal ArticleDOI
TL;DR: The performance of the newly developed biocatalyst to degrade Bisphenol A (BPA) from aqueous solutions was tested and Fourier-transform Infrared (FTIR) spectroscopy suggested BPA transformation by laccase.

177 citations

Journal ArticleDOI
16 Sep 2017
TL;DR: The present review provides exhaustive information of bacterial laccases reported till date including sources, production conditions, characterization, cloning and biotechnological applications needed for the effective understanding and application of these enzymes at the industrial level.
Abstract: Laccases (benzenediol: oxygen oxidoreductase, EC 1.10.3.2) are multi-copper enzymes which catalyze the oxidation of a wide range of phenolic and non-phenolic aromatic compounds in the presence or absence of a mediator. Till date, laccases have mostly been isolated from fungi and plants, whereas laccase from bacteria has not been well studied. Bacterial laccases have several unique properties that are not characteristics of fungal laccases such as stability at high temperature and high pH. Bacteria produce these enzymes either extracellularly or intracellularly and their activity is in a wide range of temperature and pH. It has application in pulp biobleaching, bioremediation, textile dye decolorization, pollutant degradation, biosensors, etc. Hence, comprehensive information including sources, production conditions, characterization, cloning and biotechnological applications is needed for the effective understanding and application of these enzymes at the industrial level. The present review provides exhaustive information of bacterial laccases reported till date.

175 citations


Cites background from "Recent developments in the use of t..."

  • ...Some of these dyes become recalcitrant against various environmental (temperature, light, pH) and biological (microorganisms) factors (Chandra and Chowdhary 2015; Shi et al. 2015a, b; Ba and Kumar 2017)....

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References
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Journal ArticleDOI
TL;DR: Copper sites have historically been divided into three classes based on their spectroscopic features, which reflect the geometric and electronic structure of the active site: type 1 or blue copper, type 2 (T2) or normal copper, and type 3 (T3) or coupled binuclear copper centers.
Abstract: Copper is an essential trace element in living systems, present in the parts per million concentration range. It is a key cofactor in a diverse array of biological oxidation-reduction reactions. These involve either outer-sphere electron transfer, as in the blue copper proteins and the Cu{sub A} site of cytochrome oxidase and nitrous oxide redutase, or inner-sphere electron transfer in the binding, activation, and reduction of dioxygen, superoxide, nitrite, and nitrous oxide. Copper sites have historically been divided into three classes based on their spectroscopic features, which reflect the geometric and electronic structure of the active site: type 1 (T1) or blue copper, type 2 (T2) or normal copper, and type 3 (T3) or coupled binuclear copper centers. 428 refs.

3,241 citations


"Recent developments in the use of t..." refers background in this paper

  • ...(b) Admitted catalytic reaction of Lac with diphenol to phenoxy radical formation (adapted from [11])....

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  • ...light and heavy MW, respectively) [11]....

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Journal ArticleDOI
TL;DR: The fact that laccases only require molecular oxygen for catalysis makes them suitable for biotechnological applications for the transformation or immobilization of xenobiotic compounds.
Abstract: Laccases of fungi attract considerable attention due to their possible involvement in the transformation of a wide variety of phenolic compounds including the polymeric lignin and humic substances. So far, more than a 100 enzymes have been purified from fungal cultures and characterized in terms of their biochemical and catalytic properties. Most ligninolytic fungal species produce constitutively at least one laccase isoenzyme and laccases are also dominant among ligninolytic enzymes in the soil environment. The fact that they only require molecular oxygen for catalysis makes them suitable for biotechnological applications for the transformation or immobilization of xenobiotic compounds.

1,925 citations


"Recent developments in the use of t..." refers background in this paper

  • ...At the latter site, accumulated electrons enable the reduction of oxygen to water [38]....

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Journal ArticleDOI
TL;DR: Different methods for the immobilization of enzymes are critically reviewed, with emphasis on relatively recent developments, such as the use of novel supports, e.g., mesoporous silicas, hydrogels, and smart polymers, novel entrapment methods and cross-linked enzyme aggregates (CLEAs).
Abstract: Immobilization is often the key to optimizing the operational performance of an enzyme in industrial processes, particularly for use in non-aqueous media. Different methods for the immobilization of enzymes are critically reviewed. The methods are divided into three main categories, viz. (i) binding to a prefabricated support (carrier), (ii) entrapment in organic or inorganic polymer matrices, and (iii) cross-linking of enzyme molecules. Emphasis is placed on relatively recent developments, such as the use of novel supports, e.g., mesoporous silicas, hydrogels, and smart polymers, novel entrapment methods and cross-linked enzyme aggregates (CLEAs).

1,857 citations


"Recent developments in the use of t..." refers methods in this paper

  • ...The main advantages of the method include easy recovery of enzymes as well as products, employing fewer unit operations and less solvent usage with small bioreactor volume [34,35]....

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Journal ArticleDOI
TL;DR: The advantages and disadvantages of the different existing immobilization strategies to solve the different aforementioned enzyme limitations are given and some advice to select the optimal strategy for each particular enzyme and process is given.
Abstract: Enzyme biocatalysis plays a very relevant role in the development of many chemical industries, e.g., energy, food or fine chemistry. To achieve this goal, enzyme immobilization is a usual pre-requisite as a solution to get reusable biocatalysts and thus decrease the price of this relatively expensive compound. However, a proper immobilization technique may permit far more than to get a reusable enzyme; it may be used to improve enzyme performance by improving some enzyme limitations: enzyme purity, stability (including the possibility of enzyme reactivation), activity, specificity, selectivity, or inhibitions. Among the diverse immobilization techniques, the use of pre-existing supports to immobilize enzymes (via covalent or physical coupling) and the immobilization without supports [enzyme crosslinked aggregates (CLEAs) or crystals (CLECs)] are the most used or promising ones. This paper intends to give the advantages and disadvantages of the different existing immobilization strategies to solve the different aforementioned enzyme limitations. Moreover, the use of nanoparticles as immobilization supports is achieving an increasing importance, as the nanoparticles versatility increases and becomes more accessible to the researchers. We will also discuss here some of the advantages and drawbacks of these non porous supports compared to conventional porous supports. Although there are no universal optimal solutions for all cases, we will try to give some advice to select the optimal strategy for each particular enzyme and process, considering the enzyme properties, nature of the process and of the substrate. In some occasions the selection will be compulsory, for example due to the nature of the substrate. In other cases the optimal biocatalyst may depend on the company requirements (e.g., volumetric activity, enzyme stability, etc).

1,378 citations

Journal ArticleDOI

1,117 citations


"Recent developments in the use of t..." refers background in this paper

  • ...oxy (Cu–O2–Cu ) and met (Cu–Cu) states [19] which define the catalytic cycle of the enzyme and its reaction mechanism with substrates as illustrated for fungal Tyr in Figure 3(a)....

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