Enhancing the thermal stability of lipases through mutagenesis and immobilization on zeolites |
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Authors: | L Costa V Brissos F Lemos F Ramôa Ribeiro J M S Cabral |
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Institution: | (1) IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisbon, Portugal |
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Abstract: | The hydrolysis reaction of p-nitrophenyl butyrate catalyzed by lipases was followed with in situ UV/vis diode array spectrophotometry. Five enzymes -
Candida antarctica lipase B and Fusarium solani pisi cutinase wild-type and three single-mutation variants - were tested as catalysts in homogeneous conditions and immobilized
on zeolite NaY, on a polyacrylate support and as cross-linked aggregates. Using deconvolution techniques and kinetic modeling,
the thermal stability of the different biocatalysts was compared in operational conditions and the results were supported
by steady-state enzyme fluorescence measurements. We concluded that both the mutagenesis and the immobilization on zeolite
NaY had a positive effect on the thermal stability of F. solani pisi cutinase. |
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Keywords: | Lipase Thermal stability Zeolite NaY Mutagenesis Steady-state fluorescence |
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