INVESTIGADORES
CERMINATI Sebastian
artículos
Título:
The βγ-crystallin domain of Lysinibacillus sphaericus phosphatidylinositol phospholipase C plays a central role in protein stability
Autor/es:
CERMINATI, SEBASTIÁN; PAOLETTI, LUCIANA; PEIRÚ, SALVADOR; MENZELLA, HUGO G.; CASTELLI, MARÍA EUGENIA
Revista:
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Editorial:
SPRINGER
Referencias:
Año: 2018
ISSN:
0175-7598
Resumen:
βγ-crystallin has emerged as a superfamily of structurally homologous proteins with representatives across all domains of life. A major portion of this superfamily is constituted by microbial members. This superfamily has also been recognized as a novel group of Ca2+-binding proteins with a large diversity and variable properties in Ca2+ binding and stability. We have recently described a new phosphatidylinositol phospholipase C from Lysinibacillus sphaericus (LS-PIPLC) which was shown to efficiently remove phosphatidylinositol from crude vegetable oil. Here, the role of the C-terminal βγ-crystallin domain of LS-PIPLC was analyzed in the context of the whole protein. A truncated protein in which the C-terminal βγ-crystallin domain was deleted (LS-PIPLCΔCRY) is catalytically as efficient as the full-length protein (LS-PIPLC). However, the thermal and chemical stability of LS-PIPLCΔCRYare highly affected, demonstrating a stabilizing role for this domain. It is also shown that the presence of Ca2+ increases the thermal and chemical stability of the protein both in aqueous media and in oil, making LS-PIPLC an excellent candidate for use in industrial soybean oil degumming.