Bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistance
Abstract Manganese peroxidase (MnP) is in increasing demand due to its ability to degrade straw lignin and facilitate the conversion of agricultural waste into valuable feed resources. However, free MnP faces limitations in industrial applications owing to high operational costs, poor stability, and...
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| Format: | Article |
| Language: | English |
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SpringerOpen
2025-06-01
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| Series: | Bioresources and Bioprocessing |
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| Online Access: | https://doi.org/10.1186/s40643-025-00901-9 |
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| author | Lu He Mati Ullah Muhammad Naeem Zhong Ni Yong Feng Tawaf Ali Shah Molalign Assefa Khalid S. Almaary Huayou Chen |
| author_facet | Lu He Mati Ullah Muhammad Naeem Zhong Ni Yong Feng Tawaf Ali Shah Molalign Assefa Khalid S. Almaary Huayou Chen |
| author_sort | Lu He |
| collection | DOAJ |
| description | Abstract Manganese peroxidase (MnP) is in increasing demand due to its ability to degrade straw lignin and facilitate the conversion of agricultural waste into valuable feed resources. However, free MnP faces limitations in industrial applications owing to high operational costs, poor stability, and poor resistance to environmental stressors. In this study, MnP derived from Irpex lacteus was displayed on the surface of Bacillus subtilis spores using the cotB protein as an anchor molecule. Compared with refolded MnP expressed in E. coli, the spore-displayed MnP exhibited superior acid resistance, with an optimal pH of 3.5 (compared to pH 4.0 for the free enzyme). Additionally, the immobilized enzyme CotB-MnP retained 73.9% of its initial activity after incubation at 30℃ for 1 h incubation. Notably, immobilization eliminated the inhibitory effects of K⁺ and Zn²⁺ ions, which instead promoted the activity of the spore-displayed enzyme. The reusable spores maintained 69% of their initial activity after three consecutive cycles, highlighting their potential for industrial straw feed processing. Graphical Abstract |
| format | Article |
| id | doaj-art-a3002ed69aed4e02b63fd998a793e260 |
| institution | OA Journals |
| issn | 2197-4365 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | Bioresources and Bioprocessing |
| spelling | doaj-art-a3002ed69aed4e02b63fd998a793e2602025-08-20T02:06:23ZengSpringerOpenBioresources and Bioprocessing2197-43652025-06-0112111410.1186/s40643-025-00901-9Bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistanceLu He0Mati Ullah1Muhammad Naeem2Zhong Ni3Yong Feng4Tawaf Ali Shah5Molalign Assefa6Khalid S. Almaary7Huayou Chen8School of the Life Sciences, Jiangsu UniversitySchool of the Life Sciences, Jiangsu UniversitySchool of the Life Sciences, Jiangsu UniversitySchool of the Life Sciences, Jiangsu UniversitySchool of the Life Sciences, Jiangsu UniversityCollege of Agriculture Engineering and Food Science, Shandong University of TechnologySouthern Agricultural Research Institute, Werabe Agricultural Research CenterDepartment of Botany and Microbiology, College of Science, King Saud UniversitySchool of the Life Sciences, Jiangsu UniversityAbstract Manganese peroxidase (MnP) is in increasing demand due to its ability to degrade straw lignin and facilitate the conversion of agricultural waste into valuable feed resources. However, free MnP faces limitations in industrial applications owing to high operational costs, poor stability, and poor resistance to environmental stressors. In this study, MnP derived from Irpex lacteus was displayed on the surface of Bacillus subtilis spores using the cotB protein as an anchor molecule. Compared with refolded MnP expressed in E. coli, the spore-displayed MnP exhibited superior acid resistance, with an optimal pH of 3.5 (compared to pH 4.0 for the free enzyme). Additionally, the immobilized enzyme CotB-MnP retained 73.9% of its initial activity after incubation at 30℃ for 1 h incubation. Notably, immobilization eliminated the inhibitory effects of K⁺ and Zn²⁺ ions, which instead promoted the activity of the spore-displayed enzyme. The reusable spores maintained 69% of their initial activity after three consecutive cycles, highlighting their potential for industrial straw feed processing. Graphical Abstracthttps://doi.org/10.1186/s40643-025-00901-9Manganese peroxidaseSpore surface displayStress tolerance |
| spellingShingle | Lu He Mati Ullah Muhammad Naeem Zhong Ni Yong Feng Tawaf Ali Shah Molalign Assefa Khalid S. Almaary Huayou Chen Bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistance Bioresources and Bioprocessing Manganese peroxidase Spore surface display Stress tolerance |
| title | Bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistance |
| title_full | Bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistance |
| title_fullStr | Bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistance |
| title_full_unstemmed | Bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistance |
| title_short | Bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistance |
| title_sort | bacillus subtilis spore surface display enhances manganese peroxidase stability and stress resistance |
| topic | Manganese peroxidase Spore surface display Stress tolerance |
| url | https://doi.org/10.1186/s40643-025-00901-9 |
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