Immobilization on octyl-agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica
Autor: | Roberto Fernandez-Lafuente, Sara Arana-Peña, Yuliya Lokha |
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Rok vydání: | 2018 |
Předmět: |
0106 biological sciences
Acetonitriles Immobilized enzyme 01 natural sciences Catalysis Dioxanes Fungal Proteins chemistry.chemical_compound 010608 biotechnology Polyethyleneimine Lipase Triacetin Candida Polyethylenimine Chromatography biology 010401 analytical chemistry biology.organism_classification Enzymes Immobilized Enzyme assay 0104 chemical sciences Butyrates chemistry Biocatalysis biology.protein Agarose Candida antarctica Biotechnology |
Zdroj: | Biotechnology progress. 35(1) |
ISSN: | 1520-6033 |
Popis: | Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl-agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobilized on the same support, as both enzymes are among the most popular ones used in biocatalysis. CALA immobilization produced a significant increase in enzyme activity vs. p-nitrophenyl butyrate (pNPB) (by a factor of seven), and the coating with PEI did not have a significant effect on enzyme activity. CALB reduced its activity slightly after enzyme immobilization. Octyl-CALA was less stable than octyl-CALB at pH 9 and more stable at pH 5 and, more clearly, at pH 7. PEI coating only increased octyl-CALA stability at pH 9. In organic solvents, CALB had much better stability in methanol and was similarly stable in acetonitrile or dioxane. In these systems, the PEI coating of octyl-CALA permitted some stabilization. While octyl-CALA was more active vs. pNPB, octyl-CALB was much more active vs. mandelic esters or triacetin. Thus, depending on the specific reaction and the conditions, CALA or CALB may offer different advantages and drawbacks. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 35: e2735, 2019. |
Databáze: | OpenAIRE |
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