The βγ-crystallin domain of Lysinibacillus sphaericus phosphatidylinositol phospholipase C plays a central role in protein stability.

Autor: Cerminati S; CONICET y Departamento de Tecnología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Procesos Biotecnológicos y Químicos (IPROBYQ), Universidad Nacional de Rosario (UNR), Suipacha 531, 2000, Rosario, Argentina., Paoletti L; CONICET y Departamento de Tecnología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Procesos Biotecnológicos y Químicos (IPROBYQ), Universidad Nacional de Rosario (UNR), Suipacha 531, 2000, Rosario, Argentina., Peirú S; CONICET y Departamento de Tecnología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Procesos Biotecnológicos y Químicos (IPROBYQ), Universidad Nacional de Rosario (UNR), Suipacha 531, 2000, Rosario, Argentina., Menzella HG; CONICET y Departamento de Tecnología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Procesos Biotecnológicos y Químicos (IPROBYQ), Universidad Nacional de Rosario (UNR), Suipacha 531, 2000, Rosario, Argentina., Castelli ME; CONICET y Departamento de Tecnología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Procesos Biotecnológicos y Químicos (IPROBYQ), Universidad Nacional de Rosario (UNR), Suipacha 531, 2000, Rosario, Argentina. castelli@iprobyq-conicet.gob.ar.
Jazyk: angličtina
Zdroj: Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2018 Aug; Vol. 102 (16), pp. 6997-7005. Date of Electronic Publication: 2018 Jun 16.
DOI: 10.1007/s00253-018-9136-9
Abstrakt: 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 Ca 2+ -binding proteins with a large diversity and variable properties in Ca 2+ 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-PIPLC ΔCRY ) is catalytically as efficient as the full-length protein (LS-PIPLC). However, the thermal and chemical stability of LS-PIPLC ΔCRY are highly affected, demonstrating a stabilizing role for this domain. It is also shown that the presence of Ca 2+ 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.
Databáze: MEDLINE
Externí odkaz:
Nepřihlášeným uživatelům se plný text nezobrazuje