Bioeconomy Science Institute, AgResearch Group
Browse

Current understanding on the heterogenous expression of de-polymerizing enzymes in <i>Pichia pastoris</i>

Download (1.24 MB)
journal contribution
posted on 2025-01-23, 19:59 authored by Shuyan WuShuyan Wu, David HooksDavid Hooks, Gale BrightwellGale Brightwell
<p dir="ltr">Enzymatic depolymerisation is increasingly recognised as a reliable and environmentally friendly method. The development of this technology hinges on the availability of high-quality enzymes and associated bioreaction systems for upscaling biodegradation. Microbial heterologous expression systems have been studied for meeting this demand. Among these systems, the <i>Pichia pastoris</i> expression system has emerged as a widely used platform for producing secreted heterologous proteins. This article provides an overview of studies involving the recombinant expression of polymer-degrading enzymes using the <i>P. pastoris</i> expression system. Research on <i>P. pastoris</i> expression of interested enzymes with depolymerising ability, including cutinase, lipase, and laccase, are highlighted in the review. The key factors influencing the heterologous expression of polymer-degrading enzymes in <i>P. pastoris</i> are discussed, shedding light on the challenges and opportunities in the development of depolymerising biocatalysts through the <i>P. pastoris</i> expression system.</p>

Funding

AgResearch Strategic Science Investment Fund

History

Rights statement

© 2025 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

Publication date

2025-01-14

Project number

  • PRJ0760857

Language

  • English

Does this contain Māori information or data?

  • No

Publisher

MDPI

Journal title

Bioengineering

ISSN

2306-5354

Volume/issue number

12(1)

Page numbers

68

Usage metrics

    Licence

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC