Use of laccase in pulp and paper industry

Virk, Antar Puneet; Sharma, Prince; Capalash, Neena

doi:10.1002/btpr.727

Cited by 122 publications

(62 citation statements)

References 71 publications

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“…Furthermore, some of these pretreatments produce inhibitors that decrease the overall yield of the fermentation process (7). In this context, laccases have drawn much attention in past decades as an ecological alternative for many processes in the biotechnology industries (11)(12)(13)(14). Laccases, which facilitate the degradation of lignin, can largely contribute to current efforts to overcome limitations of enzymatic degradation of lignocellulosic biomass.…”

Section: Discussionmentioning

confidence: 99%

“…Laccases (EC 1.10.3.2) are wellstudied blue multicopper oxidases (type 1) found in fungi, plants, and microorganisms that catalyze the oxidation of a wide variety of phenolic and nonphenolic compounds, with concomitant reduction of molecular oxygen to water (8)(9)(10). The broad substrate range of laccases allows their use in numerous types of industrial and biotechnological fields, such as the paper, textile, and food industries (11)(12)(13)(14). Known functions of fungal (15) and bacterial (16) laccases include roles in morphogenesis, sporulation, and pigmentation.…”

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confidence: 99%

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Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome

Davidi

Moraïs

Artzi

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Efficient breakdown of lignocellulose polymers into simple molecules is a key technological bottleneck limiting the production of plant-derived biofuels and chemicals. In nature, plant biomass degradation is achieved by the action of a wide range of microbial enzymes. In aerobic microorganisms, these enzymes are secreted as discrete elements in contrast to certain anaerobic bacteria, where they are assembled into large multienzyme complexes termed cellulosomes. These complexes allow for very efficient hydrolysis of cellulose and hemicellulose due to the spatial proximity of synergistically acting enzymes and to the limited diffusion of the enzymes and their products. Recently, designer cellulosomes have been developed to incorporate foreign enzymatic activities in cellulosomes so as to enhance lignocellulose hydrolysis further. In this study, we complemented a cellulosome active on cellulose and hemicellulose by addition of an enzyme active on lignin. To do so, we designed a dockerin-fused variant of a recently characterized laccase from the aerobic bacterium Thermobifida fusca. The resultant chimera exhibited activity levels similar to the wild-type enzyme and properly integrated into the designer cellulosome. The resulting complex yielded a twofold increase in the amount of reducing sugars released from wheat straw compared with the same system lacking the laccase. The unorthodox use of aerobic enzymes in designer cellulosome machinery effects simultaneous degradation of the three major components of the plant cell wall (cellulose, hemicellulose, and lignin), paving the way for more efficient lignocellulose conversion into soluble sugars en route to alternative fuels production.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome

Davidi

Moraïs

Artzi

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…Hydratases break a CC π bond in the middle of the alkyl chain and attach a hydroxyl group at one of the carbons (Joo et al 2012). Laccases convert unsaturated fatty acids into epoxy or hydroxy fatty acids (Virk et al 2012).…”

Section: Introductionmentioning

confidence: 99%

fadD deletion and fadL overexpression in Escherichia coli increase hydroxy long-chain fatty acid productivity

Bae

Park

Jung

et al. 2014

Appl Microbiol Biotechnol

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A major problem of long-chain fatty acid (LCFA) hydroxylation using Escherichia coli is that FadD (long-chain fatty acyl-CoA synthetase), which is necessary for exogenous LCFA transport, also initiates cellular consumption of LCFA. In this study, an effective method to prevent the cellular consumption of LCFA without impairing its transport is proposed. The main idea is that a heterologous enzyme which consumes LCFA can replace FadD in LCFA transport. For the model heterologous enzyme, CYP153A from Marinobacter aquaeolei, which converts palmitic acid into ω-hydroxy palmitic acid, was expressed in E. coli. When fadD was deleted from an E. coli strain, CYP153A indeed maintained the ability to transport LCFA. A disadvantage of fadD deletion mutant is the fact that FadD deficiency downregulates the transcription of fadL (outer membrane LCFA transporter) via FadR (fatty acid metabolism regulator protein), was solved by fadL overexpression from a plasmid. In addition, the overexpression of fadL was able to offset catabolite repression on fadL, allowing glucose to be used as the primary carbon source. In conclusion, the strain with fadD deletion and fadL overexpression showed 5.5-fold increase in productivity compared to the wild-type strain, converting 2.6 g/L (10.0 mM) of palmitic acid into 2.4 g/L (8.8 mM) of ω-hydroxy palmitic acid in a shake flask. This simple genetic manipulation can be applied to any LCFA hydroxylation using E. coli.

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“…Some of these applications are already in practice, such as pulp processing (Virk et al 2012), detoxification of environmental pollutants (Harms et al 2011), preventing wine browning (Osma et al 2010), oxidation of dyes and their precursors (Kumar et al 2011), and producing lignin from cellulosic material (Wang et al 2014). Laccase has been used commercially as a potential delignification agent in pulp production since the last decade (Camarero et al 2007;Rico et al 2014;Wang et al 2014).…”

Section: Laccase Application In Fiberboard Fabricationmentioning

confidence: 99%

Laccase, an Emerging Tool to Fabricate Green Composites: A Review

Mahmood¹,

Hashim²,

Sulaiman³

et al. 2015

BioResources

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In the last two decades, laccases have received much attention from researchers because of their specific ability to oxidize lignin. This function of laccase is very useful for applications in several biotechnological processes, including delignification in the pulp and paper industry and the detoxification of industrial effluents from the textile and petrochemical industries. This review focuses on laccase-mediated fiberboard synthesis. Growing concerns regarding the emission of formaldehyde from wood composites has prompted industrialists to consider the fabrication of green composites. Laccase-mediated fiber treatments oxidize the lignin component without affecting the cellulose structure. As a result, free radicals are generated on the fiber surface, and these can act as potential reactive sites for further cross-linking reactions in board manufacturing. Binderless fiberboards prepared using such methods can be considered as green composites because the manufacturing process involves no additional resin.

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Use of laccase in pulp and paper industry

Cited by 122 publications

References 71 publications

Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome

Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome

fadD deletion and fadL overexpression in Escherichia coli increase hydroxy long-chain fatty acid productivity

Laccase, an Emerging Tool to Fabricate Green Composites: A Review

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