Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis
IntroductionThe 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...
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Frontiers Media S.A.
2024-12-01
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| Series: | Frontiers in Sustainable Food Systems |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fsufs.2024.1465445/full |
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| author | Jiang Huang Jiang Huang Jun Wang Jun Wang Jinling He Jinling He Yupeng Wu Yupeng Wu Lizhi Chen Lizhi Chen Shuangzi Zhou Shuangzi Zhou Yeyu Bian Yeyu Bian Yangyuan Li Yangyuan Li |
| author_facet | Jiang Huang Jiang Huang Jun Wang Jun Wang Jinling He Jinling He Yupeng Wu Yupeng Wu Lizhi Chen Lizhi Chen Shuangzi Zhou Shuangzi Zhou Yeyu Bian Yeyu Bian Yangyuan Li Yangyuan Li |
| author_sort | Jiang Huang |
| collection | DOAJ |
| description | IntroductionThe 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.MethodsWe 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 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.Results and discussionWe 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. 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. |
| format | Article |
| id | doaj-art-6ad247ae7b7a453ab49a7e78e3714aea |
| institution | OA Journals |
| issn | 2571-581X |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Sustainable Food Systems |
| spelling | doaj-art-6ad247ae7b7a453ab49a7e78e3714aea2025-08-20T02:19:54ZengFrontiers Media S.A.Frontiers in Sustainable Food Systems2571-581X2024-12-01810.3389/fsufs.2024.14654451465445Enhanced production of thermostable catalase for efficient gluconic acid biocatalysisJiang Huang0Jiang Huang1Jun Wang2Jun Wang3Jinling He4Jinling He5Yupeng Wu6Yupeng Wu7Lizhi Chen8Lizhi Chen9Shuangzi Zhou10Shuangzi Zhou11Yeyu Bian12Yeyu Bian13Yangyuan Li14Yangyuan Li15Guangdong Vtr Bio-Tech Co., Ltd., Zhuhai, Guangdong, ChinaGuangdong Feed Additive Research and Development Center, Zhuhai, Guangdong, ChinaGuangdong Vtr Bio-Tech Co., Ltd., Zhuhai, Guangdong, ChinaGuangdong Feed Additive Research and Development Center, Zhuhai, Guangdong, ChinaGuangdong Vtr Bio-Tech Co., Ltd., Zhuhai, Guangdong, ChinaGuangdong Feed Additive Research and Development Center, Zhuhai, Guangdong, ChinaGuangdong Vtr Bio-Tech Co., Ltd., Zhuhai, Guangdong, ChinaGuangdong Feed Additive Research and Development Center, Zhuhai, Guangdong, ChinaGuangdong Vtr Bio-Tech Co., Ltd., Zhuhai, Guangdong, ChinaGuangdong Feed Additive Research and Development Center, Zhuhai, Guangdong, ChinaGuangdong Vtr Bio-Tech Co., Ltd., Zhuhai, Guangdong, ChinaGuangdong Feed Additive Research and Development Center, Zhuhai, Guangdong, ChinaGuangdong Vtr Bio-Tech Co., Ltd., Zhuhai, Guangdong, ChinaGuangdong Feed Additive Research and Development Center, Zhuhai, Guangdong, ChinaGuangdong Vtr Bio-Tech Co., Ltd., Zhuhai, Guangdong, ChinaGuangdong Feed Additive Research and Development Center, Zhuhai, Guangdong, ChinaIntroductionThe 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.MethodsWe 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 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.Results and discussionWe 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. 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.https://www.frontiersin.org/articles/10.3389/fsufs.2024.1465445/fullcatalaseAspergillus nigergluconic acidthermal stabilitysignal peptideheme |
| spellingShingle | Jiang Huang Jiang Huang Jun Wang Jun Wang Jinling He Jinling He Yupeng Wu Yupeng Wu Lizhi Chen Lizhi Chen Shuangzi Zhou Shuangzi Zhou Yeyu Bian Yeyu Bian Yangyuan Li Yangyuan Li Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis Frontiers in Sustainable Food Systems catalase Aspergillus niger gluconic acid thermal stability signal peptide heme |
| title | Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis |
| title_full | Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis |
| title_fullStr | Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis |
| title_full_unstemmed | Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis |
| title_short | Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis |
| title_sort | enhanced production of thermostable catalase for efficient gluconic acid biocatalysis |
| topic | catalase Aspergillus niger gluconic acid thermal stability signal peptide heme |
| url | https://www.frontiersin.org/articles/10.3389/fsufs.2024.1465445/full |
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