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RevistaEnzyme and Microbial Technology
Año2020
Volumen133
Páginas109461
Internacional

MODULATING THE PROPERTIES OF THE LIPASE FROM Thermomyces lanuginosus IMMOBILIZED ON OCTYL AGAROSE BEADS BY ALTERING THE IMMOBILIZATION CONDITIONS

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Yuliya Lokha1,+,  Sara Arana-Peña1,+, Nathalia S. Rios1,2, Carmen Mendez- Sanchez1, Luciana R. B. Gonçalves2, Fernando Lopez-Gallego3,4 and Roberto Fernandez-Lafuente1,*



The lipase from Thermomyces lanuginosus (TLL) has been immobilized on octyl-agarose beads via interfacial activation under 16 different conditions (changing the immobilization pH, the ionic strength, the presence of additives like calcium, phosphate or glycerol) and using a low loading (1 mg/g support). Then, the properties of the different biocatalysts have been evaluated: stability at pH 7.0 and 70ºC and activity versus p-nitro phenyl propionate, triacetin and R- and S- methyl mandelate. Results clearly indicate that the immobilization conditions determine the final enzyme properties, altering enzyme stability (by 10 folds), activity (by 8 folds using R- methyl mandelate) and specificity (VR/VS changed from 0.7 to 2.3 using mandelate esters). For instance, the enzymes immobilized at pH 7.0 using 5 mM buffer were the most stable preparations, while the presence of 250 mM sodium phosphate greatly decreased the final enzyme stability. The biocatalyst stability of TLL increased with increasing NaCl in the immobilization buffer at pH 5. Fluorescence studies confirmed that the conformation of the different immobilized enzymes were different, despite being a physical and reversible immobilization method . Thus, the immobilization of TLL on octyl agarose beads under different conditions produced biocatalysts with different properties, the optimal condition depends on the studied reaction and condition.
1Departamento de Biocatálisis. ICP-CSIC, Campus UAM-CSIC, Madrid, Spain.
2Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Bloco 709, CEP 60455-760, Fortaleza, CE, Brazil.
3Heterogeneous Biocatalysis Laboratory, Instituto de Síntesis Química y Catálisis Homogénea (ISQCH-CSIC), University of Zaragoza, C/ Pedro Cerbuna 12, 50009 Zaragoza, Spain
4ARAID, Aragon I+D Foundation, Av. de Ranillas 1-D, planta 2ª, oficina B, 50018 Zaragoza, Spain
Palabras clave:lipase modulation, immobilization via interfacial activation, conformational changes, tuning lipase catalytic properties, tailoring conformational changes
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