Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Secretory Production of the Hericium erinaceus Laccase from Saccharomyces cerevisiae

  • Jin Kang (Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Thuat Van La (Department of Biosystems and Bioengineering, KRIBB School of Biotechnology, Korea National University of Science and Technology (UST)) ;
  • Mi-Jin Kim (Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Jung-Hoon Bae (Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Bong Hyun Sung (Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Seonghun Kim (Department of Biosystems and Bioengineering, KRIBB School of Biotechnology, Korea National University of Science and Technology (UST)) ;
  • Jung-Hoon Sohn (Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
  • Received : 2023.12.28
  • Accepted : 2024.01.03
  • Published : 2024.04.28
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Abstract

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 Ca2+, Zn2+, and K+ increased laccase activity, whereas 5 mM Fe2+ and Al3+ inhibited laccase activity. The laccase activity was inhibited by the addition of low concentrations of sodium azide and ⳑ-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.

Keywords

Acknowledgement

This work was supported by the National Research Foundation of Korea (NRF) grants (NRF-2022M3J5A1056169, 2021M3A9I5023254, 2019R1A2C1090726, and 2018M3A9H3024746), a National Research Council of Science & Technology grant (No. CAP20024-200) of the Korean government (MSIT) and the Research Initiative Program of KRIBB.

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