Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering
Laccase, a member of the blue multicopper oxidase family, is widely distributed across diverse taxonomic groups, including fungi, bacteria, plants, and insects. This enzyme drives biocatalytic processes through the oxidation of phenolic compounds, aromatic amines, and lignin derivatives, underpinnin...
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| Format: | Article |
| Language: | English |
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MDPI AG
2025-06-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/13/6/1422 |
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| author | Guoqiang Guan Beidian Li Ling Xu Jingya Qian Bin Zou Shuhao Huo Zhongyang Ding Kai Cui Feng Wang |
| author_facet | Guoqiang Guan Beidian Li Ling Xu Jingya Qian Bin Zou Shuhao Huo Zhongyang Ding Kai Cui Feng Wang |
| author_sort | Guoqiang Guan |
| collection | DOAJ |
| description | Laccase, a member of the blue multicopper oxidase family, is widely distributed across diverse taxonomic groups, including fungi, bacteria, plants, and insects. This enzyme drives biocatalytic processes through the oxidation of phenolic compounds, aromatic amines, and lignin derivatives, underpinning its significant potential in the food industry, cosmetics, and environmental remediation. However, wild-type laccases face critical limitations, such as low catalytic efficiency, insufficient expression yields, and poor stability. To address these bottlenecks, this review systematically examines optimization strategies for heterologous laccase expression by fungal and bacterial systems. Additionally, we discuss protein engineering for laccase modification, with a focus on the structural basis and active-site redesign. The comprehensive analysis presented herein provides strategic suggestions for advancing laccase engineering, ultimately establishing a theoretical framework for developing high-efficiency, low-cost engineered variants for large-scale biomanufacturing and green chemistry applications. |
| format | Article |
| id | doaj-art-54368d25dfb94e42bb00950014f7fddf |
| institution | Matheson Library |
| issn | 2076-2607 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj-art-54368d25dfb94e42bb00950014f7fddf2025-06-25T14:12:51ZengMDPI AGMicroorganisms2076-26072025-06-01136142210.3390/microorganisms13061422Improving the Properties of Laccase Through Heterologous Expression and Protein EngineeringGuoqiang Guan0Beidian Li1Ling Xu2Jingya Qian3Bin Zou4Shuhao Huo5Zhongyang Ding6Kai Cui7Feng Wang8School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, ChinaInstitute of Feed Research, Chinese Academy of Agricultural Sciences, Beijing 100081, ChinaSchool of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, ChinaLaccase, a member of the blue multicopper oxidase family, is widely distributed across diverse taxonomic groups, including fungi, bacteria, plants, and insects. This enzyme drives biocatalytic processes through the oxidation of phenolic compounds, aromatic amines, and lignin derivatives, underpinning its significant potential in the food industry, cosmetics, and environmental remediation. However, wild-type laccases face critical limitations, such as low catalytic efficiency, insufficient expression yields, and poor stability. To address these bottlenecks, this review systematically examines optimization strategies for heterologous laccase expression by fungal and bacterial systems. Additionally, we discuss protein engineering for laccase modification, with a focus on the structural basis and active-site redesign. The comprehensive analysis presented herein provides strategic suggestions for advancing laccase engineering, ultimately establishing a theoretical framework for developing high-efficiency, low-cost engineered variants for large-scale biomanufacturing and green chemistry applications.https://www.mdpi.com/2076-2607/13/6/1422laccaseheterologous expressionfungibacteriaenzyme engineering |
| spellingShingle | Guoqiang Guan Beidian Li Ling Xu Jingya Qian Bin Zou Shuhao Huo Zhongyang Ding Kai Cui Feng Wang Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering Microorganisms laccase heterologous expression fungi bacteria enzyme engineering |
| title | Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering |
| title_full | Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering |
| title_fullStr | Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering |
| title_full_unstemmed | Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering |
| title_short | Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering |
| title_sort | improving the properties of laccase through heterologous expression and protein engineering |
| topic | laccase heterologous expression fungi bacteria enzyme engineering |
| url | https://www.mdpi.com/2076-2607/13/6/1422 |
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