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Published on: February 11, 2019
Structural stability of Staphylococcus xylosus lipase is modulated by Zn(2+) ions
Jean Borges Bertoldo1, Guilherme Razzera, Javier Vernal
1Departamento de Bioquímica, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, Florianópolis, SC, Brazil.
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.
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