Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance
Backgrounds: Glycerolysis, with its advantages of readily available raw materials, simple operation, and mild reaction conditions, is a primary method for producing diacylglycerol (DAG). However, enzymatic glycerolysis faces challenges such as high enzyme costs, low reuse efficiency, and poor stabil...
| Main Authors: | , , , , , , |
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| Format: | Article |
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John Wiley and Sons Ltd
2024
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| Online Access: | http://psasir.upm.edu.my/id/eprint/114252/ |
| _version_ | 1848866439042170880 |
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| author | Xie, Rui Peng, Xianwu Lee, Yee-Ying Xie, Pengkai Tan, Chin-Ping Wang, Yong Zhang, Zhen |
| author_facet | Xie, Rui Peng, Xianwu Lee, Yee-Ying Xie, Pengkai Tan, Chin-Ping Wang, Yong Zhang, Zhen |
| author_sort | Xie, Rui |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Backgrounds: Glycerolysis, with its advantages of readily available raw materials, simple operation, and mild reaction conditions, is a primary method for producing diacylglycerol (DAG). However, enzymatic glycerolysis faces challenges such as high enzyme costs, low reuse efficiency, and poor stability. The study aims to develop a cost-effective immobilized enzyme by covalently binding lipase to pre-activated carriers through the selection of suitable lipases, carriers, and activating agents. The optimization is intended to improve the glycerolysis reaction for efficient DAG production.
Results: Lipase CN-TL (from Thermomyces lanuginosus) was selected through glycerolysis reaction and molecular docking to catalyze the glycerolysis reaction. Optimizing the immobilization method by covalently binding CN-TL to poly(ethylene glycol) diglycidyl ether (PEGDGE)-preactivated resin LX-201A resulted in the preparation of the immobilized enzyme TL-PEGDGE-LX. The immobilized enzyme retained over 90% of its initial activity after five consecutive reactions, demonstrating excellent reusability. The DAG content in the product remained at 84.8% of its initial level, further highlighting the enzyme's potential for reusability and its promising applications in the food and oil industries.
Conclusions: The immobilized lipase TL-PEGDGE-LX, created by covalently immobilizing lipase CN-TL on PEGDGE-preactivated carriers, demonstrated broad applicability and excellent reusability. This approach offers an economical and convenient immobilization strategy for the enzymatic glycerolysis production of DAG. © 2024 Society of Chemical Industry. |
| first_indexed | 2025-11-15T14:20:37Z |
| format | Article |
| id | upm-114252 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T14:20:37Z |
| publishDate | 2024 |
| publisher | John Wiley and Sons Ltd |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1142522025-01-10T03:17:40Z http://psasir.upm.edu.my/id/eprint/114252/ Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance Xie, Rui Peng, Xianwu Lee, Yee-Ying Xie, Pengkai Tan, Chin-Ping Wang, Yong Zhang, Zhen Backgrounds: Glycerolysis, with its advantages of readily available raw materials, simple operation, and mild reaction conditions, is a primary method for producing diacylglycerol (DAG). However, enzymatic glycerolysis faces challenges such as high enzyme costs, low reuse efficiency, and poor stability. The study aims to develop a cost-effective immobilized enzyme by covalently binding lipase to pre-activated carriers through the selection of suitable lipases, carriers, and activating agents. The optimization is intended to improve the glycerolysis reaction for efficient DAG production. Results: Lipase CN-TL (from Thermomyces lanuginosus) was selected through glycerolysis reaction and molecular docking to catalyze the glycerolysis reaction. Optimizing the immobilization method by covalently binding CN-TL to poly(ethylene glycol) diglycidyl ether (PEGDGE)-preactivated resin LX-201A resulted in the preparation of the immobilized enzyme TL-PEGDGE-LX. The immobilized enzyme retained over 90% of its initial activity after five consecutive reactions, demonstrating excellent reusability. The DAG content in the product remained at 84.8% of its initial level, further highlighting the enzyme's potential for reusability and its promising applications in the food and oil industries. Conclusions: The immobilized lipase TL-PEGDGE-LX, created by covalently immobilizing lipase CN-TL on PEGDGE-preactivated carriers, demonstrated broad applicability and excellent reusability. This approach offers an economical and convenient immobilization strategy for the enzymatic glycerolysis production of DAG. © 2024 Society of Chemical Industry. John Wiley and Sons Ltd 2024-09-11 Article PeerReviewed Xie, Rui and Peng, Xianwu and Lee, Yee-Ying and Xie, Pengkai and Tan, Chin-Ping and Wang, Yong and Zhang, Zhen (2024) Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance. Journal of the Science of Food and Agriculture, 105 (2). pp. 816-828. ISSN 0022-5142; eISSN: 1097-0010 https://scijournals.onlinelibrary.wiley.com/doi/10.1002/jsfa.13872 10.1002/jsfa.13872 |
| spellingShingle | Xie, Rui Peng, Xianwu Lee, Yee-Ying Xie, Pengkai Tan, Chin-Ping Wang, Yong Zhang, Zhen Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance |
| title | Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance |
| title_full | Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance |
| title_fullStr | Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance |
| title_full_unstemmed | Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance |
| title_short | Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance |
| title_sort | enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance |
| url | http://psasir.upm.edu.my/id/eprint/114252/ http://psasir.upm.edu.my/id/eprint/114252/ http://psasir.upm.edu.my/id/eprint/114252/ |