التفاصيل البيبلوغرافية
| العنوان: |
A novel hybrid biocatalyst from immobilized Eversa® Transform 2.0 lipase and its application in biolubricant synthesis. |
| المؤلفون: |
Germano de Sousa, Isamayra, Valério Chaves, Anderson, de Oliveira, André Luiz Barros, da Silva Moreira, Katerine, Gonçalves de Sousa Junior, Paulo, Simão Neto, Francisco, Cristina Freitas de Carvalho, Simone, Bussons Rodrigues Valério, Roberta, Vieira Lima, Gledson, Sanders Lopes, Ada Amélia, Martins de Souza, Maria Cristiane, da Fonseca, Aluísio Marques, Fechine, Pierre Basílio Almeida, de Mattos, Marcos Carlos, dos Santos, José C. S. |
| المصدر: |
Biocatalysis & Biotransformation; Apr2024, Vol. 42 Issue 2, p151-172, 22p |
| مصطلحات موضوعية: |
LIPASES, GLUTARALDEHYDE, ENZYMES, FOURIER transform infrared spectroscopy, ORGANIC solvents, IONIC strength |
| مستخلص: |
In this study, a Taguchi experimental design was used for optimzing the immobilization of the lipase Eversa® Transform 2.0 (EVS) onto a hybrid support consisting of chitosan (CHI) and agarose (AGA), with glutaraldehyde (GLU) used as the support activator. The biocatalyst obtained was characterized by X-Ray Diffraction (XRD), Fourier Transform Infrared Spectroscopy (FTIR), Thermogravimetry (TGA), Energy Dispersive Spectroscopy (EDS), and Scanning Electron Microscopy (SEM). The optimized reaction conditions (60 min, 5 mM ionic strength, 1% GLU concentration, and 5 mg protein load per g of support) resulted in a highly active biocatalyst (74.39 ± 0.48 U/g) and delivered an immobilization yield of 74.20 ± 0.28%. The biocatalyst produced was observed to lose only 15.3% of its activity after 61 days of storage. The activity was also observed to increase by 96.70% ± 0.76, 27.34% ± 2.34, and 84.35% ± 1.68 in the presence of the organic solvents hexane, cyclohexane, and methanol, respectively. Additionally, the byocatalist showed more pronounced activity at temperatures above 50 °C and was still able to retain approximately 30% of it at 70 °C. These values were found to be higher at alkaline pHs, as the activity of Eversa® 2.0 Transform saw an increase of up to 140% at pH 9. The desorption tests performed did not reveal any enzymatic detachment from the support. The novel biocatalyst also showed promising ester-lubricating properties. Furthermore, the in silico study revealed a binding affinity of −5.1 kcal/mol between oleic acid and the enzyme, suggesting that the combination of the substrate and the lipase was more stable and therefore, suitable for esterification. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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