Bio-ceramic, mesoporous cuttlebone of Sepia officinalis is an ideal support for the immobilization of Bacillus subtilis AKL13 lipase: optimization, adsorption, thermodynamic and reaction kinetic studies
| Autor: | Karthikumar Sankar, Anant Achary |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Langmuir
biology Immobilized enzyme Chemistry General Chemical Engineering 02 engineering and technology General Chemistry Bacillus subtilis 010402 general chemistry 021001 nanoscience & nanotechnology biology.organism_classification 01 natural sciences Biochemistry Industrial and Manufacturing Engineering 0104 chemical sciences Hydrolysis Adsorption Materials Chemistry biology.protein Lipase 0210 nano-technology Mesoporous material Nuclear chemistry Thermostability |
| Zdroj: | Chemical Papers. 74:459-470 |
| ISSN: | 1336-9075 2585-7290 |
| Popis: | Mesoporous cuttlebone powder of Sepia officinalis (CBP) was characterized and used as matrix for the immobilization of Bacillus subtilis AKL 13 lipase (BsL). Particle size and surface area of the matrix used for enzyme immobilization were 89.95 µm and 1.631 m2 g−1, respectively. Remarkable thermostability (54% of weight loss at 700 °C) of CBP was determined in TGA profile. The lipase immobilization process parameters were sequentially optimized by response surface methodology followed by artificial neural network and genetic algorithm. The maximum lipase loading capacity of CBP was 255 mg g−1 of support. Immobilized lipase (CBP-BsL) showed maximum specific activity of 5808 U mg−1 of protein in p-nitrophenol palmitate hydrolysis. Adsorption isotherm study revealed that the binding of lipase on the surface of CBP was Langmuir and the binding was physical adsorption. CBP-BsL showed lower activation energy (51.4 KJ mol−1) and higher thermal stability with half-lives of 13.3 h at 50 °C. Higher activity retention in nonpolar solvents and 69% of operational stability after 15 cycle of reaction were measured. |
| Databáze: | OpenAIRE |
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