INSTITUTO DE PROCESOS BIOTECNOLOGICOS Y QUIMICOS ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
?Functional charachterization of the βγ-crystallin domain of a phosphatidylinositol phospholipase C from Lysinobacillus sphaericus?
CERMINATI, SEBASTIAN; MENZELLA H. G.; PEIRU, SALVADOR; PAOLETTI, LUCIANA; CASTELLI, MARÍA EUGENIA
Congreso; SAIB 2018; 2018
βγ-crystallins have emerged as a superfamily of structurally homologous proteins with representatives across all the domains of life. A majorportion of this superfamily is constituted by members from microorganisms. This superfamily has also been recognized as a novel group of Ca2+-binding proteins with huge diversity and variable properties in Ca2+-binding, stability and association with other domains.We have recently described the development of a new phosphatidylinositol (PI) phospholipase C from Lysinobacillussphaericus (LS-PI-PLC) tobe used for oil degumming which was shown to efficiently remove PI from crude oil. Here, the role of the C-terminal βγ-crystallin domain of LS-PI-PLC is analyzed in the context of the whole protein. A truncated protein in which the C-terminal βγ-crystallin domain was deleted (LS-PI-PLCΔCRY) is catalytically as efficient as the full-length protein (LS-PI-PLC). However, the thermal and chemical stability of LS-PIPLCΔCRY arehighly affected, demonstrating a stabilizing role for this domain. It is also shown that the presence of Ca2+ increases the thermal and chemicalstability of the protein both in aqueous media and in oil, making LS-PI-PLC an excellent candidate for use in industrial soybean oil degumming.