Biosynthesis of benzyl cinnamate using an efficient immobilized lipase entrapped in nano-molecular cages
| Autor: | Gao-Ying Zhi, Yi-Ping Cao, Dong-Hao Zhang, Li Han, Queting Chen |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
01 natural sciences
Analytical Chemistry Catalysis chemistry.chemical_compound 0404 agricultural biotechnology Biosynthesis Benzyl Compounds Enzyme Stability Native state Organic chemistry Denaturation (biochemistry) Lipase chemistry.chemical_classification biology 010401 analytical chemistry technology industry and agriculture 04 agricultural and veterinary sciences General Medicine Hydrogen-Ion Concentration Enzymes Immobilized 040401 food science 0104 chemical sciences Enzyme chemistry Cinnamates Yield (chemistry) biology.protein Benzyl cinnamate Food Science |
| Zdroj: | Food Chemistry. 364:130428 |
| ISSN: | 0308-8146 |
| DOI: | 10.1016/j.foodchem.2021.130428 |
| Popis: | To improve the performance of lipase in biosynthesis of benzyl cinnamate, a new immobilized lipase by entrapping enzyme into nano-molecular cages was designed. Consequently, the entrapped lipase showed a robust immobilization, which diminished the leakage of lipase notably in use. Moreover, the entrapped lipase exhibited higher activity (57.1 U/mg) than free lipase (50.0 U/mg), demonstrating that the native conformation of lipase was not destroyed during immobilization. Compared with the adsorbed lipase (half-life 40.7 min) and free lipase (half-life 29.8 min), the entrapped lipase (half-life 85.3 min) increased the stability by about 2–3 times. Furthermore, the entrapped lipase was applied in biosynthesis of benzyl cinnamate, where it showed excellent activity and re-usability. After 7 cycles, the yield of benzyl cinnamate catalyzed by the entrapped lipase remained 70.2%, while the yield catalyzed by the adsorbed lipase was only about 10%. These results indicated that the nano-molecular cages could inhibit denaturation of lipase and maintain its activity well. |
| Databáze: | OpenAIRE |
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