title: Structural stability of Staphylococcus xylosus lipase is modulated by Zn(2+) ions.
abstract: Lipases are well-known enzymes extensively used in industrial biotransformation processes. Besides, their structural and catalytic characteristics have attracted increasing attention of several industries in the last years. In this work, we used biophysical and molecular modeling tools to assess structural properties of Staphylococcus xylosus lipase (SXL). We studied the thermal unfolding of this protein and its zinc-dependent thermotolerance. We demonstrated that SXL is able to be active and stable at moderate temperatures, but this feature is only acquired in the presence of Zn(2+). Such characteristic indicates SXL as a zinc-dependent metallolipase.
authors.affiliation: Departamento de Bioquímica, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, Florianópolis, SC, Brazil.
authors.forename: Jean Borges
authors.initials: JB
authors.lastname: Bertoldo
authors.forename: Guilherme
authors.initials: G
authors.lastname: Razzera
authors.forename: Javier
authors.initials: J
authors.lastname: Vernal
authors.forename: Fábio Cristiano Angonesi
authors.initials: FC
authors.lastname: Brod
authors.forename: Ana Carolina Maisonnave
authors.initials: AC
authors.lastname: Arisi
authors.forename: Hernán
authors.initials: H
authors.lastname: Terenzi
mesh_terms: D000595:Amino Acid Sequence; D004795:Enzyme Stability; D008049:Lipase / Q000737:chemistry*; D008066:Lipolysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D013210:Staphylococcus / Q000201:enzymology*; D015032:Zinc / Q000737:chemistry*
chemical_list: D008049:Lipase; D015032:Zinc