An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst
Abstract Lipase represents one of the most important industrial biocatalysts, with a global market value of $590.5 million by 2020. However, their catalytic efficiency is often hindered by a closed “lid” conformation. Here, we present an aggregation-induced conformation locking strategy that enables...
Saved in:
| Main Authors: | , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-05-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-59824-w |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850268694598385664 |
|---|---|
| author | Anlian Huang Zhi-Wei Li Lihong Guo Ningyi Zhong Linjing Tong Yanbin Xu Xiaomin Ma Fang Zhu Guosheng Chen Siming Huang Gangfeng Ouyang |
| author_facet | Anlian Huang Zhi-Wei Li Lihong Guo Ningyi Zhong Linjing Tong Yanbin Xu Xiaomin Ma Fang Zhu Guosheng Chen Siming Huang Gangfeng Ouyang |
| author_sort | Anlian Huang |
| collection | DOAJ |
| description | Abstract Lipase represents one of the most important industrial biocatalysts, with a global market value of $590.5 million by 2020. However, their catalytic efficiency is often hindered by a closed “lid” conformation. Here, we present an aggregation-induced conformation locking strategy that enables the facile synthesis of highly activated lipase hybrid biocatalysts. Lipase is self-activated into an open-lid conformation via solvent-mediated aggregation, followed by conformational locking within a two-dimensional metal-organic framework (MOF). The resulting MOF biocatalyst provides high accessibility to the locked lipase aggregates through its long-range ordered pore channels, achieving a hydrolytic efficiency 5.30 times greater than that of native lipase. To the best of our knowledge, this represents a record-high activation efficiency for ester hydrolysis among the reported lipase-based hybrid biocatalysts to date. We also demonstrate its feasibility to catalytically accelerate transesterification and esterification reactions, showing up to as 6.64 times higher yield than native lipase and impressive recyclability. |
| format | Article |
| id | doaj-art-67bfcb835ab54042a04a4d07b455c2ec |
| institution | OA Journals |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-67bfcb835ab54042a04a4d07b455c2ec2025-08-20T01:53:23ZengNature PortfolioNature Communications2041-17232025-05-0116111310.1038/s41467-025-59824-wAn aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalystAnlian Huang0Zhi-Wei Li1Lihong Guo2Ningyi Zhong3Linjing Tong4Yanbin Xu5Xiaomin Ma6Fang Zhu7Guosheng Chen8Siming Huang9Gangfeng Ouyang10MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen UniversityMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen UniversityMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen UniversityMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen UniversityMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen UniversityGuangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences, Guangzhou Medical UniversityShenzhen Medical Academy of Research and TranslationMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen UniversityMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen UniversityGuangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences, Guangzhou Medical UniversityMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen UniversityAbstract Lipase represents one of the most important industrial biocatalysts, with a global market value of $590.5 million by 2020. However, their catalytic efficiency is often hindered by a closed “lid” conformation. Here, we present an aggregation-induced conformation locking strategy that enables the facile synthesis of highly activated lipase hybrid biocatalysts. Lipase is self-activated into an open-lid conformation via solvent-mediated aggregation, followed by conformational locking within a two-dimensional metal-organic framework (MOF). The resulting MOF biocatalyst provides high accessibility to the locked lipase aggregates through its long-range ordered pore channels, achieving a hydrolytic efficiency 5.30 times greater than that of native lipase. To the best of our knowledge, this represents a record-high activation efficiency for ester hydrolysis among the reported lipase-based hybrid biocatalysts to date. We also demonstrate its feasibility to catalytically accelerate transesterification and esterification reactions, showing up to as 6.64 times higher yield than native lipase and impressive recyclability.https://doi.org/10.1038/s41467-025-59824-w |
| spellingShingle | Anlian Huang Zhi-Wei Li Lihong Guo Ningyi Zhong Linjing Tong Yanbin Xu Xiaomin Ma Fang Zhu Guosheng Chen Siming Huang Gangfeng Ouyang An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst Nature Communications |
| title | An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst |
| title_full | An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst |
| title_fullStr | An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst |
| title_full_unstemmed | An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst |
| title_short | An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst |
| title_sort | aggregation induced conformation locking strategy facilitates the activation of lipase biocatalyst |
| url | https://doi.org/10.1038/s41467-025-59824-w |
| work_keys_str_mv | AT anlianhuang anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT zhiweili anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT lihongguo anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT ningyizhong anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT linjingtong anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT yanbinxu anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT xiaominma anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT fangzhu anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT guoshengchen anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT siminghuang anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT gangfengouyang anaggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT anlianhuang aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT zhiweili aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT lihongguo aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT ningyizhong aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT linjingtong aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT yanbinxu aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT xiaominma aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT fangzhu aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT guoshengchen aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT siminghuang aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst AT gangfengouyang aggregationinducedconformationlockingstrategyfacilitatestheactivationoflipasebiocatalyst |