A number of oxidative enzymes from bacteria, fungi and plants have been reported to play an important role in numerous waste treatment applications. Peroxidases and/or phenoloxidases can act on specific recalcitrant pollutants by precipitation or transforming to other products and permitting a better final treatment of the waste. Improvement in the useful life and thereby a reduction in treatment cost has been accomplished through enzyme immobilization. Horseradish peroxidase, lignin peroxidase and manganese peroxidase mineralize a variety of recalcitrant aromatic compounds. Immobilization of these enzymes on porous ceramic supports or resins did not adversely affect their stability and showed a good potential for degradation of environment persistent aromatics. Tyrosinase, which catalyzes the hydroxylation of phenols and dehydrogenation of o-diphenols, in an immobilized form exerted an excellent phenol removal. Laccase is capable of eliminating the phenols through polymerization process, however, the presence of mediator such as ABTS and HBT degraded phenol by oxidative process. Many applications with oxidative enzymes and plant materials in effluent as in soil remediation will be discussed.

Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment: a review

(Received 17 October 2000/Accepted 12 April 2001) The sources of ligninocellulose that occur in various forms in nature are so vast that they can only be compared to those of water. The results of several, more recent experiments showed that laccase probably possesses the big ability for "lignin-barrier" breakdown of ligninocellulose. The degradation of this compound is currently understood as an enzymatic process mediated by small molecules, therefore, this review will focus on the role of these mediators and radicals working in concert with enzymes. The fungi having a versatile machinery of enzymes are able to attack directly the "lignin- barrier" or can use a multienzyme system including "feed-back" type enzymes allowing for simulta- neous transformation of lignin and carbohydrate compounds.

Fungal laccase: properties and activity on lignin

Introduction
Historical Outline
Bacteria and Microfungi
Actinomycetes
Other Bacteria
Soft-Rot Fungi and Other Microfungi


Brown-Rot Basidiomycetes
White-Rot Basidiomycetes
Mineralization of 14C-Labeled Lignins
Ligninolytic Enzymes


Catabolism of Primary Degradation Products
Outlook and Perspectives
Patents


Keywords:

lignin;
wood;
lignocellulose;
white-rot fungi;
brown-rot fungi;
soft-rot fungi;
actinomycetes;
lignin peroxidase;
manganese peroxidase;
laccase;
molecular biology;
radicals;
mediators;
manganese;
veratryl alcohol;
oxalate;
vanillic acid

Biodegradation of Lignin

Laccases are blue multicopper oxidases, which catalyze the monoelectronic oxidation of a broad spectrum of substrates, for example, ortho- and para-diphenols, polyphenols, aminophenols, and aromatic or aliphatic amines, coupled with a full, four-electron reduction of O2 to H2O. Hence, they are capable of degrading lignin and are present abundantly in many white-rot fungi. Laccases decolorize and detoxify the industrial effluents and help in wastewater treatment. They act on both phenolic and nonphenolic lignin-related compounds as well as highly recalcitrant environmental pollutants, and they can be effectively used in paper and pulp industries, textile industries, xenobiotic degradation, and bioremediation and act as biosensors. Recently, laccase has been applied to nanobiotechnology, which is an increasing research field, and catalyzes electron transfer reactions without additional cofactors. Several techniques have been developed for the immobilization of biomolecule such as micropatterning, self-assembled monolayer, and layer-by-layer techniques, which immobilize laccase and preserve their enzymatic activity. In this review, we describe the fungal source of laccases and their application in environment protection.

https://downloads.hindawi.com/archive/2014/163242.pdf

Fungal Laccases and Their Applications in Bioremediation

Laccases are an interesting group of multi copper enzymes, which have received much attention of researchers in last decades due to their ability to oxidize both phenolic and non-phenolic lignin related compounds as well as highly recalcitrant environmental pollutants. This makes these biocatalysts very useful for their application in several biotechnological processes. Such applications include the detoxification of industrial effluents, mostly from the paper and pulp, textile and petrochemical industries, polymer synthesis, bioremediation of contaminated soils, wine and beverage stabilization. Laccases are also used as catalysts for the manufacture of anti-cancer drugs and even as ingredients in cosmetics. Recently, the utility of laccases has also been applied to nanobiotechnology. This paper reviews recent and important patents related to the properties, heterologous production, molecular cloning, and applications of laccases within different industrial fields as well as their potential extension to the nanobiotechnology area.

/pdf/laccases-and-their-applications-a-patent-review-23hct8y4o0.pdf

Laccases and their applications: a patent review.

The extracellular laccase of white rot fungus Cerrena unicolor was purified from culture by ion-exchange chromatography on DEAE-Toyopearl column and immobilized on silanized porous glass heads. During bonding procedure 94.35% protein and 100 % laccase activity were coupled to the support. Optimum pH for immobilized laccase compared to free enzyme was shifted from 5.5 to 5.7. The immobilized laccase was more resistant for thermal denaturation: at 70°C, the activity of immobilized enzyme was around 20 % higher than that of the free enzyme. It was also more stable during storage at 4°C. After about seven months the immobilized laccase retained 94.81 % of its initial activity, whereas free enzyme only 39.59 %. Nine water-miscible organic solvents tested in an anhydrous form caused an inhibitory effect on both laccase forms, but, in the mixture with water, the enzyme in all cases shows activity. It decreased, however, when the concentration of solvents increased. Among all solvents, the best results were obtained with ethylene glycol and methoxyethanol. When the reaction mixture contained 50 % of ethylene glycol, free and immobilized laccase retained 24 and 31 % respectively of their activity in the buffer. In the case of 50 % methoxyethanol these data were 6 and 36 %. Organic solvents shifted pH optima of both laccase forms to pH 6.0. The calculation from Lineweaver-Burk plot oxidizing capacity of laccase towards syringaldazine was slightly higher for the free enzyme than for immobilized one, 18.5 and 20.0 M/l respectively. These results show that Cerrena unicolor laccase both in free and immobilized form is able to catalyze the oxidation of syringaldazine in organic solvents. It may be usable in transformation of substrates insoluble or sparingly soluble in water. The immobilized laccase, as more stable and temperature resistant than free enzyme, seems to be more useful.

Activity of Free and Immobilized Extracellular Cerrena unicolor Laccase in Water Miscible Organic Solvents

Screening of the wood-rotting fungi for laccase production: Induction by ferulic acid, partial purification, and immobilization of laccase from the high laccase-producing strain, Cerrena unicolor

Appearance of Laccase in Wood - Rotting Fungi and Its Inducibility

Purification of extracellular Cerrena unicolor laccase by means of affinity chromatography

친화크로마토그래프법을 이용한 Cerrena Unicolor Laccase의 정제특성 ( Purification of Extracellular Cerrena Unicolor Laccase by Means of Affinity Chromatography )

Handle everyday research tasks with reliable, citation-backed results

Your personal Research Agent to handle research tasks with citation-backed results

Popular Tasks used by Researchers

How can I help with your research?

Meet SciSpace

Get more enhanced response by uploading the PDFs you want me to reference.

No relevant PDFs in your library

SciSpace is the AI research assistant for academics. Run systematic literature reviews on 280M+ papers, and write papers with cited sources. Trusted by 1M+ students, PhDs & researchers.

SciSpace | AI for Research

Analyze PDFs

Code & Manuscripts

Funding & Grants

Literature & Patents

Medical & Clinical Data

Systematic Review

Visualize & Present

Web & Data

Build a Google Scholar-like website for your research.

Build a website

Create charts and images for your research

Create a Chart

Write a paper for submission to a journal

Draft a manuscript

Patent Search

Design eye-catching scientific posters in minutes.

Scientific Poster Generation

Systematic Literature Review

One task is running at the moment. Your messages will be shown right after.

Drag and drop or click here to browse

Loved by <highlight>1 million+</highlight> researchers

Extract a list of specific topics and their sources from unstructured text

Topics

Compare and analyze relevant papers that matches with your search

Papers

Get insights from PDFs and bookmarked papers from your library

My library

Recent searches

Try searching for:

Catch AI-generated content in scholarly and non-scholarly content

{ai} Detector

Ai Writer

Get PDF Summaries, highlighted text explanations 

Chat with PDF

Effortlessly create in-text citations and bibliographies in APA and 2,500 other formats

Citation generator

Get explanations, summaries, and answers on academic papers

Ease up your research workflow with {scispace}'s cohort of exciting AI tools

Elevate your academic writing skills and convey your ideas the way you want

Paraphraser

Explore our range of reading and writing tools

Your file is being prepared and should be ready in a few minutes. If it's a large file, it might take a bit longer. You can close this window, and we'll email you the file when it's done.

You have reached a maximum limit of <strong>{limit}</strong> columns in the table. Remove at least <strong>1</strong> column to add or create another one.

L. Gianfreda

Author Tools

Chat about Author