PROIMI   05436
PLANTA PILOTO DE PROCESOS INDUSTRIALES MICROBIOLOGICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
The brighter side of amyloid aggregation: biological nanotubes as support for enzyme photo-immobilization.
Autor/es:
SILVINA CHAVES, CINTIA M ROMERO, FLORENCIA GONZALEZ LIZARRAGA, CLAUDIO D. BORSARELLI , LICIA M PERA, MARIO BAIGORI AND ROSANA CHEHÍN
Lugar:
San Miguel de Tucuman
Reunión:
Congreso; SAB; 2012
Resumen:
The brighter side of amyloid aggregation: biological nanotubes as support for enzyme photo-immobilization. RESERVADO SAB Silvina Chaves1, Cintia M Romero2, Florencia Gonzalez Lizarraga1, Claudio D. Borsarelli3 , Licia M Pera2, Mario Baigori2 and Rosana Chehín1. 1Instituto Superior de Investigaciones Biológicas (INSIBIO), CCT-Tucumán and Insitituto de Química Biológica Dr Bernabé Bloj (CONICET-UNT) Chacabuco 461 (T4000ILI) Tucumán, 2PROIMI, PROIMI-CONICET, Av. Belgrano y Pasaje Caseros, T4001 MVB, Tucumán, Argentina. Fac Bioq, Qca y Farmacia (UNT), Ayacucho 461, 4000, Tucumán. 3 Centro de Investigaciones y Transferencia de Santiago del Estero (CITSE-CONICET). U.N. de Santiago del Estero. RN9 Km1125, 4206-Sgo del Estero Amyloid fibrils are highly ordered protein aggregates which are formed through a self-assembly process when a protein is converted into a cross β-structure in which sheet?sheet interactions are perpendicular to the fibril axis. It is now widely known that the ability to form amyloid fibrils is a common property of polypeptides, although efficient preparation of amyloid fibrils is difficult to achieve for most proteins. Nowaday, fibrils have attracted growing interest as new biomaterials due to their high mechanical, chemical, and structural properties. In the present work, we report the covalent photo-immobilization of a microbial lipase (EC 3.1.1.3) from Brevibacillus agri, onto amyloid fibrils prepared from lysozyme by using a photosensitization technique with visible light. The lipase activity was retained upon photo-attachment and centrifugation. Successful immobilization was determined using electrophoresis, and lipase activity assay. Lipases catalyze hydrolysis of triglycerides at oil?water interfaces. This is a reversible reaction and the enzyme also catalyzes ester synthesis under microaqueous conditions. The catalytic activity of lipases was tested by hydrolysis of p-nitrophenyl palmitate (pNPP). Using amyloid fibrils, we have obtained photo-immobilized lipases in a single-step, clean and fast fashion, and with remarkable efficiency that were assessed based on activity, stability, robustness, and reusability. The immobilized lipase on amyloid fibrils was able to catalyze hydrolysis and synthesis reactions. These results could acquire relevance in the biotechnological uses of amyloid aggregation as an immobilization platform can lead to the development of a new type of immobilized catalysts. Agradecimientos: This work was supported by grants CIUNT 26/D409; CIUNT 26/D239 (UNT), PIP 297 (CONICET), CICyT-UNSE 23A/133 and ANPCyT (PICT-06-01090).