1. Academic Validation
  2. Development of novel recombinant peroxidase secretion system from Pseudomonas putida for lignin valorisation

Development of novel recombinant peroxidase secretion system from Pseudomonas putida for lignin valorisation

  • Bioresour Technol. 2023 Nov:388:129779. doi: 10.1016/j.biortech.2023.129779.
Siseon Lee 1 Minsik Kang 2 Chan-Duck Jung 3 Jung-Hoon Bae 1 Ju Young Lee 3 Young-Kwon Park 4 Jeong Chan Joo 5 Hoyong Kim 3 Jung-Hoon Sohn 2 Bong Hyun Sung 6
Affiliations

Affiliations

  • 1 Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Republic of Korea.
  • 2 Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Republic of Korea; Biosystems and Bioengineering Program, Korea University of Science and Technology (UST), Daejeon 34113, Republic of Korea.
  • 3 Center for Bio-based Chemistry, Korea Research Institute of Chemical Technology (KRICT), Ulsan 44429, Republic of Korea.
  • 4 School of Environmental Engineering, University of Seoul, Seoul 02504, Republic of Korea.
  • 5 Department of Biotechnology, The Catholic University of Korea, Bucheon-si, Gyeonggi-do 14662, Republic of Korea.
  • 6 Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Republic of Korea; Biosystems and Bioengineering Program, Korea University of Science and Technology (UST), Daejeon 34113, Republic of Korea; Graduate School of Engineering Biology, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Republic of Korea. Electronic address: bhsung@kribb.re.kr.
Abstract

Pseudomonas putida is a promising strain for lignin valorisation. However, there is a dearth of stable and efficient systems for secreting Enzymes to enhance the process. Therefore, a novel secretion system for recombinant lignin-depolymerising peroxidase was developed. By adopting a flagellar type III secretion system, P. putida KT-M2, a secretory host strain, was constructed and an optimal secretion signal fusion partner was identified. Application of the dye-decolourising peroxidase of P. putida to this system resulted in efficient oxidation activity of the cell-free supernatant against various chemicals, including lignin model compounds. This peroxidase-secreting strain was examined to confirm its lignin utilisation capability, resulting in the efficient assimilation of various lignin substrates with 2.6-fold higher growth than that of the wild-type strain after 72 h of cultivation. Finally, this novel system will lead efficient Bacterial lignin breakdown and utilization through enzyme secretion, paving the way for sustainable lignin-consolidated bioprocessing.

Keywords

DyP-type peroxidase; Enzyme secretion; Flagellar Type III secretion; Lignin valorization; Pseudomonas putida.

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