Isolation of a laccase-coding gene from the lignin-degrading fungus<i>Phlebia brevispora</i>BAFC 633 and heterologous expression in<i>Pichia pastoris</i>

Fonseca, María Isabel; Molina, M.; Winnik, D L; Busi, María V.; Fariña, Julia Inés; Villalba, Laura Lidia; Zapata, Pedro Darío

doi:10.1111/jam.13720

Cited by 22 publications

(16 citation statements)

References 66 publications

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“…Then, we can elucidate that more than six histidine tags at the amino region interfered with lac-case activity. Supporting our results, Fonseca et al (2018) obtained similar levels of recombinant laccase expressed in Pichia pastoris cloning with primers with a polyhistidine tag.…”

Section: Heterologous Expression Of Laccasesupporting

confidence: 84%

“…For amplification and purification, 20 ng of DNA plasmid containing the coding region of the laccase gene, previously obtained by Fonseca et al (2018), was used. PCR amplifications were carried out using the cycling standardized by the working group (Fonseca et al, 2018). All fragments were separated by electrophoresis on 2% (w/v) agarose gel in 0.5× TBE buffer and stained with red gel.…”

Section: Amplificationmentioning

confidence: 99%

“…3.0−4.5 (Fonseca et al, 2018;Li et al, 2013;Tülek et al, 2021;Zhuo et al, 2015). Laccase enzyme was stable at 40 • C, which is crucial during the biotechnological process (Fonseca et al, 2014).…”

Section: Characterization Of Laccase Enzymementioning

confidence: 99%

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Purification and characterization of a fungal laccase expressed in Kluyveromyces lactis suitable for baking

Molina

Cazzaniga

Milde

et al. 2023

Journal of Food Science

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Laccase enzyme can replace chemical additives to improve texture properties and the volume of bread. Laccase encoding gene from Phlebia brevispora, a native fungus from Misiones, Argentina, was expressed in the generally recognized as safe yeast Kluyveromyces lactis. To improve laccase activity, medium conditions were optimized. The use of iron sulfate at a concentration of 1 mM led to optimum laccase activity (1289 U·L−1) on the fourth day of incubation. SDS‐PAGE analysis revealed that the molecular mass of purified laccase was about 180 kDa. Optimum pH for the enzyme was 4 and optimum temperature was 40°C. Laccase exhibited high stability at low pH and high temperature. The application of recombinant laccase to bread decreased hardness, gumminess, and chewiness and increased bread volume. Based on these results, recombinant laccase from P. brevispora with improved yield is a good option for application as an improver of the physicochemical quality of bread at the industrial level. Besides, it will allow us to advance toward our goal of developing healthy alternatives for the bakery industry. No previous work has been reported concerning the heterologous expression of the laccase gene native to the province of Misiones, Argentina, with an aim for application in baking. Practical Application Healthy bakeries became a trend in recent years. The use of the laccase enzyme increases the specific volume and decreases the hardness of bread, being thus an alternative for the replacement of chemical additives in the bakery industry.

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Section: Heterologous Expression Of Laccasesupporting

confidence: 84%

Section: Amplificationmentioning

confidence: 99%

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Purification and characterization of a fungal laccase expressed in Kluyveromyces lactis suitable for baking

Molina

Cazzaniga

Milde

et al. 2023

Journal of Food Science

Self Cite

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“…Meanwhile, the selection of appropriate lignocellulosic biomass for fungus growth and enzyme production plays an important role in the development of efficient biotechnology (Elisashvili et al 2008;Han et al 2021a). There have been few studies on laccase related to the genus Phlebia, and previous studies were mainly focused on the effect of chemical and metallic compounds on laccase or the heterologous expression of a laccase gene (Kaneko et al 2009;Fonseca et al 2014Fonseca et al , 2018Janusz et al 2016). However, the effect of lignocellulosic biomass on laccase activity from the genus Phlebia has not been reported.…”

Section: Statistical Analysis Resultsmentioning

confidence: 99%

Laccase activities from three white-rot fungal species isolated from their native habitat in North China using solid-state fermentation with lignocellulosic biomass

Liu

Zhao

et al. 2022

BioRes

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Laccase has huge potential application in all aspects of biotechnology due to the ability of laccase to oxidize a wide range of phenolic and non-phenolic compounds. The future success of such applications requires large amounts of laccase with low costs. White-rot fungi are important groups of laccase production. In this study, three white-rot fungi, Phlebia acerina Han 618, Trametes hirsuta Han 726, and Coriolopsis trogii Han 751, isolated from a native North China habitat, were identified by the method of molecular biology and preliminary screening of the ability of laccase-production by guaiacol selection medium. Then they were fermented on different lignocellulosic biomass. Three species showed consistency in preference of lignocellulosic biomass, and the presence of stalk of Sorghum bicolor was more suitable for secreting laccase. The capacity of laccase secretion from different species was significantly different. The capacity of secreting laccase of C. trogii Han 751 was superior to that of P. acerina Han 618 and T. hirsuta Han 726. The discovery of a new strain with superior capacity of secreting laccase and suitable lignocellulosic biomass were helpful for laying a foundation for the optimization of the fermentation conditions for the highest laccase production, the isolation and purification of laccase, and the industrial application of laccase.

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“…Gene was converted into Pichia pastoris for protein expression. Consequences showed that the enzyme created by lac I had a good solvent/salt tolerance, demonstrating that it might be used in a variety of biotechnological applications [64]. Jin et al [65] stated the identification of the lac I gene from Ganoderma tsugae, which was found to have the ligninolytic capacity in knockout tests.…”

Section: Lignin Depolymerization From Enzymes Produced By Fungimentioning

confidence: 99%

Transforming Lignin Biomass to Value: Interplay Between Ligninolytic Enzymes and Lignocellulose Depolymerization

Ahmad¹,

Aslam²,

Hussain³

et al. 2022

Bioenerg. Res.

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Lignin is the main constituent of lignocellulosic biomasses, which have a significant untapped ability to replace ecologically unfavorable and non-renewable fossil fuels. The lignin is broken down by ligninolytic bacteria, which also use a peripheral pathway to transform heterogeneous lignin derivatives into central intermediates like protocatechuate or catechol. By undergoing ring cleavage through the -ketoadipate pathway, these intermediates become metabolites by producing acetyl-CoA for internal product biosynthesis, including the creation of triacylglycerols and polyhydroxyalkanoates. Expanding our understanding of ligninolytic microbial communities, strains, and enzymes through bioprospecting can help us better understand the metabolism of aromatics. The most viable idea for sustainable development is the valorization of lignin into biopolymers as well as other high-value goods. This process is now being used to generate a variety of biopolymers, including polyesters, epoxies, phenol resins, poly (lactic acids), poly hydroxyl alkanoates, and polyurethanes. Furthermore, lignin recalcitrance remained a possible barrier to efficient lignin valorization, prompting several efforts to design high-efficiency bioprocesses to produce specific polymer types as well as other important bioproducts. Graphical Abstract

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Isolation of a laccase-coding gene from the lignin-degrading fungusPhlebia brevisporaBAFC 633 and heterologous expression inPichia pastoris

Cited by 22 publications

References 66 publications

Purification and characterization of a fungal laccase expressed in Kluyveromyces lactis suitable for baking

Purification and characterization of a fungal laccase expressed in Kluyveromyces lactis suitable for baking

Laccase activities from three white-rot fungal species isolated from their native habitat in North China using solid-state fermentation with lignocellulosic biomass

Transforming Lignin Biomass to Value: Interplay Between Ligninolytic Enzymes and Lignocellulose Depolymerization

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