Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering
Identification
- Public canonical key
- radar:r-da7a7f87b6ab3ef5c068be287c475f5e
- Authors
- Guoqiang Guan · Beidian Li · Ling Xu · Jingya Qian · Bin Zou · Shuhao Huo · Zhongyang Ding · Kai Cui · Feng Wang
- Reported year
- 2025
- Reported language
- en
- Source type
- review
- First detected
- 2026-11-13T12:50:17.253341+00:00
- Last metadata observation
- 2026-11-13T12:50:17.253341+00:00
- Last HTTP verification
- Not checked
Institutions reported by the source
Jiangsu University · Jiangnan University · Chinese Academy of Agricultural Sciences · Feed Research Institute
Reported affiliation countries
CN
Documentary abstract — original language
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.
Identifiers
- OPENALEX
- https://openalex.org/W4411435942
- DOI
- 10.3390/microorganisms13061422
- PMID
- https://pubmed.ncbi.nlm.nih.gov/40572310
- PMCID
- https://www.ncbi.nlm.nih.gov/pmc/articles/12195979
Documentary context
- Documentary family
- unknown
- Source-reported types
- review
- Publishers
- Multidisciplinary Digital Publishing Institute
Entity mentions are not evidence of legal recognition. Jurisdiction studied is separate from author affiliation country.
Sources
OpenAlex · Record 1
Cite this reference
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. 2025. https://doi.org/10.3390/microorganisms13061422
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- APA
- Guoqiang Guan; Beidian Li; Ling Xu; Jingya Qian; Bin Zou; Shuhao Huo; Zhongyang Ding; Kai Cui; Feng Wang. (2025). Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering. https://doi.org/10.3390/microorganisms13061422
- Chicago
- 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. 2025. https://doi.org/10.3390/microorganisms13061422
- ISO 690
- 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. 2025. https://doi.org/10.3390/microorganisms13061422
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UDTR Global Rights of Nature Legal Library. Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering. Documentary record: https://www.declarationuniverselledesdroitsdelarbre.org/global-rights-of-nature-radar/reference/r-da7a7f87b6ab3ef5c068be287c475f5e/ · Last HTTP verification: not performed
Research dossiers and documentary relations
Source roles
Bibliographic / original publication source · https://doi.org/10.3390/microorganisms13061422
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Documentary status
Relevance pending
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