Bertoldo_2011_Biochim.Biophys.Acta_1814_1120

Reference

Title : Structural stability of Staphylococcus xylosus lipase is modulated by Zn(2+) ions - Bertoldo_2011_Biochim.Biophys.Acta_1814_1120
Author(s) : Bertoldo JB , Razzera G , Vernal J , Brod FC , Arisi AC , Terenzi H
Ref : Biochimica & Biophysica Acta , 1814 :1120 , 2011
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.
ESTHER : Bertoldo_2011_Biochim.Biophys.Acta_1814_1120
PubMedSearch : Bertoldo_2011_Biochim.Biophys.Acta_1814_1120
PubMedID: 21621655

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Citations formats

Bertoldo JB, Razzera G, Vernal J, Brod FC, Arisi AC, Terenzi H (2011)
Structural stability of Staphylococcus xylosus lipase is modulated by Zn(2+) ions
Biochimica & Biophysica Acta 1814 :1120

Bertoldo JB, Razzera G, Vernal J, Brod FC, Arisi AC, Terenzi H (2011)
Biochimica & Biophysica Acta 1814 :1120