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

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...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2018-08, Vol.102 (16), p.6997-7005
Main Authors: Cerminati, Sebastián, Paoletti, Luciana, Peirú, Salvador, Menzella, Hugo G., Castelli, María Eugenia
Format: Article
Language:English
Subjects:
Binding
Biomedical and Life Sciences
Biotechnologically Relevant Enzymes and Proteins
Biotechnology
Calcium
Calcium ions
Corrosion resistance
Crude oil
Crystal structure
Crystallin
Crystallinity
Degumming
Homology
Life Sciences
Lysinibacillus sphaericus
Microbial Genetics and Genomics
Microbiology
Microorganisms
Oils & fats
Organic chemistry
Phosphatidylinositol
Phospholipase
Phospholipase C
Proteins
Soybean oil
Soybeans
Vegetable oils
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Summary: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.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-018-9136-9