Taguchi design-assisted co-immobilization of lipase A and B from Candida antarctica onto chitosan: Characterization, kinetic resolution application, and docking studies
| Autor: | Antônio Luthierre Gama Cavalcante, Roberta Bussons Rodrigues Valério, José C. S. dos Santos, Isamayra Germano de Sousa, Gabriel Paixão de Oliveira, Gledson Vieira Lima, Aluísio Marques da Fonseca, Katerine da Silva Moreira, Maria Cristiane Martins de Souza, Anderson Valério Chaves, Marcos Carlos de Mattos, André L. B. de Oliveira, Francisco Simao Neto, Pierre Basílio Almeida Fechine, Lourembergue Saraiva de Moura Junior, Thiago de Sousa Fonseca, Daniel Morais Vieira Cruz |
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| Rok vydání: | 2022 |
| Předmět: |
biology
General Chemical Engineering Ethyl acetate General Chemistry biology.organism_classification Kinetic resolution Thermogravimetry Hydrolysis chemistry.chemical_compound chemistry biology.protein Candida antarctica Lipase Fourier transform infrared spectroscopy Enantiomeric excess Nuclear chemistry |
| Zdroj: | Chemical Engineering Research and Design. 177:223-244 |
| ISSN: | 0263-8762 |
| Popis: | In the present communication, the simultaneous co-immobilization by covalent binding of lipase A from Candida antarctica (CALA) and lipase B from Candida antarctica (CALB) in glutaraldehyde (GLU) activated chitosan (CHI) was optimized using the Taguchi method. Under optimized conditions (pH 9, 5 mM, 6:1 (protein load/g of support and 1 h), it was possible to reach 80.00 ± 0.01% for the immobilization yield (IY) and 46.01 ± 0.35 U/g for the activity of the derivative (AtD); in this case, load protein and ionic strength were the only statistically significant parameters and, therefore, those that most influenced the immobilization process. Furthermore, at pH 7, CALA-CALB-CHI had a half-life 2–6 times longer than the mixture of CALA and CALB for a temperature range of 50−80 °C. CALA-CALB showed the highest activity at pH 7, whereas CALA-CALB-CHI, except at pH 7, was more active than the soluble lipase mixture in the pH range (5–9), especially at pH 9. CHI, CHI-GLU, and CALA-CALB-CHI were characterized by X-ray powder diffraction (XRPD), Fourier Transform Infrared Spectroscopy (FTIR), Scanning Electron Microscope (SEM), Thermogravimetry (TGA), and Energy Dispersive Spectroscopy (EDS), proving the immobilization of CALA and CALB in chitosan. CALA-CALB-CHI derivative evaluated in the kinetic resolution of halohydrins acetates rac-2-bromo-1-(2-chlorophenyl) ethyl acetate (2a) and rac-2-chloro-1-(2,4-dichlorophenyl) ethyl acetate (2b), to produce the corresponding halohydrins 3a-b, which are intermediates in the synthesis of the drugs chlorprelanine (antiarrhythmic) and luliconazol (antifungal), respectively. (S)-bromohydrin 3a was obtained with 79% enantiomeric excess (ee), whereas (S)-chlorohydrin 3b produced with 98% ee, conversion of 46% and E > 200. Additionally, molecular docking was performed to elucidate the hydrolysis interaction reaction between β-halohydrin acetates and lipases CALA-CALB. |
| Databáze: | OpenAIRE |
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