Biocatalytic characterization of Hericium erinaceus laccase isoenzymes for the oxidation of lignin derivative substrates

La, Thuat Van; Sung, Bong Huyn; Kim, Seong Hun

doi:10.1016/j.ijbiomac.2023.124658

Cited by 3 publications

(4 citation statements)

References 39 publications

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“…3C ), and that for syringaldazine was pH 5.0. Similar optimum pH values for ABTS and syringaldazine have been reported for other white laccases [ 7 ]. The enzyme stability after 2 h exposure at various temperatures revealed 75% retained activity until 40°C and rapid loss of activity after 50°C ( Fig.…”

Section: Resultssupporting

confidence: 80%

“…It remains unclear as to why these two TFPs increased the secretion of the enzyme; they showed 2–3 times higher secretion than the other TFPs. For HeLac1a, which was previously discovered in H. erinaceus and expressed in P. pastoris , the increase in activity upon the addition of metal ions was not significant [ 7 ], whereas HeLac4c, secreted from S. cerevisiae , showed a metal ion-dependent increase in the activity, except for Fe and Al ions. Inhibitor assays showed that HeLac4c was more resistant to DTT than HeLac1a.…”

Section: Discussionmentioning

confidence: 99%

“…Laccase is widely distributed in plants, insects, and bacteria and is involved in lignin biosynthesis by cleaving the C-C and C-O bonds of lignin. In fungi, including mushrooms, laccases play a role in sporulation, fruiting body formation, melanin synthesis, plant pathogenicity, and in vivo degradation [ 7 ]. Many fungal laccase genes have been discovered, heterologously expressed, and characterized.…”

Section: Introductionmentioning

confidence: 99%

“…While previous efforts have explored strategies like exploring new fungal strains and optimizing growth conditions for laccase production, our research centers on a novel laccase from Hericium erinaceus , commonly known as lion’s mane mushroom [ 7 ]. Owing to the difficulty in culturing and manipulating the genes and genomes of basidiomycetes, even with CRISPR, the use of model organisms is strongly considered.…”

Section: Introductionmentioning

confidence: 99%

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Secretory Production of the Hericium erinaceus Laccase from Saccharomyces cerevisiae

Kang,

La,

Kim

et al. 2024

J. Microbiol. Biotechnol.

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Mushroom laccases play a crucial role in lignin depolymerization, one of the most critical challenges in lignin utilization. Importantly, laccases can utilize a wide range of substrates, such as toxicants and antibiotics. This study isolated a novel laccase, named HeLac4c, from endophytic white-rot fungi Hericium erinaceus mushrooms. The cDNAs for this enzyme were 1569 bp in length and encoded a protein of 523 amino acids, including a 20 amino-acid signal peptide. Active extracellular production of glycosylated laccases from Saccharomyces cerevisiae was successfully achieved by selecting an optimal translational fusion partner. We observed that 5 and 10 mM Ca 2+ , Zn 2+ , and K + increased laccase activity, whereas 5 mM Fe 2+ and Al 3+ inhibited laccase activity. The laccase activity was inhibited by the addition of low concentrations of sodium azide and L-cysteine. The optimal pH for the 2,2'-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt was 4.4. Guaiacylglycerol-β-guaiacyl ether, a lignin model compound, was polymerized by the HeLac4c enzyme. These results indicated that HeLac4c is a novel oxidase biocatalyst for the bioconversion of lignin into value-added products for environmental biotechnological applications.

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Section: Resultssupporting

confidence: 80%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Secretory Production of the Hericium erinaceus Laccase from Saccharomyces cerevisiae

Kang,

La,

Kim

et al. 2024

J. Microbiol. Biotechnol.

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Laccase: A Green Biocatalyst Offers Immense Potential for Food Industrial and Biotechnological Applications

Zhai,

Wang,

Dong

et al. 2024

J. Agric. Food Chem.

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Laccase, a multipurpose biocatalyst, is widely distributed across all kingdoms of life and plays a key role in essential biological processes such as lignin synthesis, degradation, and pigment formation. These functions are critical for fungal growth, plant-pathogen interactions, and maintenance of soil health. Due to its broad substrate specificity, multifunctional nature, and environmentally friendly characteristics, laccase is widely employed as a catalyst in various green chemistry initiatives. With its ability to oxidize a diverse range of phenolic and nonphenolic compounds, laccase has also been found to be useful as a food additive and for assessing food quality parameters. Ongoing advancements in research and technology are continually expanding the recognition of laccase's potential to address global environmental, health, and energy challenges. This review aims to provide critical insights into the applications of laccases in the biotechnology and food industry.

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Selection of organic solvents as reaction media for laccase from Trametes versicolor

Kushch,

Hordieieva,

Sirobaba

et al. 2024

Biocatalysis and Biotransformation

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Biocatalytic characterization of Hericium erinaceus laccase isoenzymes for the oxidation of lignin derivative substrates

Cited by 3 publications

References 39 publications

Secretory Production of the Hericium erinaceus Laccase from Saccharomyces cerevisiae

Secretory Production of the Hericium erinaceus Laccase from Saccharomyces cerevisiae

Laccase: A Green Biocatalyst Offers Immense Potential for Food Industrial and Biotechnological Applications

Selection of organic solvents as reaction media for laccase from Trametes versicolor

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