Skip to main content

ORIGINAL RESEARCH article

Front. Sustain. Food Syst.
Sec. Sustainable Food Processing
Volume 8 - 2024 | doi: 10.3389/fsufs.2024.1465445
This article is part of the Research Topic Comprehensive Utilization of Enzymes in Food Systems View all articles

Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis

Provisionally accepted
Jiang Huang Jiang Huang 1,2Jun Wang Jun Wang 1,2Jinling He Jinling He 1,2Yupeng Wu Yupeng Wu 1,2Lizhi Chen Lizhi Chen 1,2Shuangzi Zhou Shuangzi Zhou 1,2Yeyu Bian Yeyu Bian 1,2Yangyuan Li Yangyuan Li 1,2*
  • 1 Guangdong VTR Bio-tech Co,. Ltd, Zhuhai, Guangdong Province, China
  • 2 Guangdong Feed Additive Research and Development Center, Zhuhai, China

The final, formatted version of the article will be published soon.

    The demand for gluconic acid (GA) has risen recently, driven by its extensive applications in the food, healthcare, and construction industries. The biocatalysis of gluconic acid, facilitated by glucose oxidase and catalase, hinges on enzyme stability, significantly influencing catalytic efficiency. Nonetheless, catalase requires enhancements in thermal stability and activity to meet the requirements of practical applications. We evaluated ten catalases expressed in Aspergillus niger, ultimately selecting the catalase from the thermophilic fungus Thermoascus aurantiacus, labeled as TaCat, for its superior thermal stability and operational performance. We successfully obtained a strain with the highest catalase activity by optimizing signal peptides and overexpressing the crucial heme synthesis enzyme. Enzyme production reached an impressive 321,779.5 U/mL in a 50-L fermenter. We further characterized the enzymatic properties of the recombinant catalase, focusing on its thermostability. Simultaneously, we used AlphaFold2 for structural predictions and conducted in-depth analyses via accelerated molecular dynamics simulations. Our application studies confirmed the considerable advantages of TaCat in terms of GA production. In conclusion, TaCat, distinguished by its remarkable thermal stability and high activity, holds substantial potential for GA production.

    Keywords: Catalase, Aspergillus niger, Gluconic acid, Thermal stability, signal peptide, Heme

    Received: 16 Jul 2024; Accepted: 14 Nov 2024.

    Copyright: © 2024 Huang, Wang, He, Wu, Chen, Zhou, Bian and Li. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Yangyuan Li, Guangdong VTR Bio-tech Co,. Ltd, Zhuhai, Guangdong Province, China

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.