Fungal laccase discovered but yet undiscovered

Agrawal, Komal; Chaturvedi, Venkatesh; Verma, Pradeep

doi:10.1186/s40643-018-0190-z

Cited by 191 publications

(111 citation statements)

References 86 publications

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“…This review will focus mainly on CWLEs with degrading activity towards cellulose, hemicellulose, and pectin; further notions on CWLEs with degrading activity towards lignin, such as laccases and polyphenol-oxidases, are described in other recent reviews [12][13][14].…”

Section: Figurementioning

confidence: 99%

Green Production and Biotechnological Applications of Cell Wall Lytic Enzymes

et al. 2019

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Energy demand is constantly growing, and, nowadays, fossil fuels still play a dominant role in global energy production, despite their negative effects on air pollution and the emission of greenhouse gases, which are the main contributors to global warming. An alternative clean source of energy is represented by the lignocellulose fraction of plant cell walls, the most abundant carbon source on Earth. To obtain biofuels, lignocellulose must be efficiently converted into fermentable sugars. In this regard, the exploitation of cell wall lytic enzymes (CWLEs) produced by lignocellulolytic fungi and bacteria may be considered as an eco-friendly alternative. These organisms evolved to produce a variety of highly specific CWLEs, even if in low amounts. For an industrial use, both the identification of novel CWLEs and the optimization of sustainable CWLE-expressing biofactories are crucial. In this review, we focus on recently reported advances in the heterologous expression of CWLEs from microbial and plant expression systems as well as some of their industrial applications, including the production of biofuels from agricultural feedstock and of value-added compounds from waste materials. Moreover, since heterologous expression of CWLEs may be toxic to plant hosts, genetic strategies aimed in converting such a deleterious effect into a beneficial trait are discussed.

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Section: Figurementioning

confidence: 99%

Green Production and Biotechnological Applications of Cell Wall Lytic Enzymes

et al. 2019

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“…That is the reason why laccase is considered as a "green tool, " due to it is able to perform the catalysis process using molecular oxygen as the only co-substrate rather than hydrogen peroxide like other oxidoreductases (v.gr. lignin peroxidase and manganese peroxidase) (Agrawal et al, 2018). Laccase can cooperate with small compounds called "mediators" and oxidize non-phenolic compounds, so that its activity is not limited only to phenolic compounds (Chio et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

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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“…The molecular weight of most bacterial laccases can vary from 20 to 80 kDa [16], while for fungal laccases, this range is usually 50-80 kDa [17]. Inhibitors of laccase activity include several metals, EDTA, L-cysteine, azide, cyanide, glutathione, dithiothreitol, and thiourea, among others [18]. Recent data regarding the structural basis of laccase inhibition by metals revealed the binding of chloride and fluoride anions to the T2 copper center, and thus the inhibition of oxygen reduction [19].…”

Section: Introductionmentioning

confidence: 99%

Applications of Microbial Laccases: Patent Review of the Past Decade (2009–2019)

et al. 2019

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There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society’s increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.

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Fungal laccase discovered but yet undiscovered

Cited by 191 publications

References 86 publications

Green Production and Biotechnological Applications of Cell Wall Lytic Enzymes

Green Production and Biotechnological Applications of Cell Wall Lytic Enzymes

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

Applications of Microbial Laccases: Patent Review of the Past Decade (2009–2019)

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