TY - JOUR 
A1 - Molina Espeja, Patricia
AU - Santos Moriano, Paloma Carmen
AU - García Ruiz, Eva
AU - Ballesteros, Antonio O.
AU - Plou, Francisco J.
AU - Alcalde, Miguel
T1 - Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase
Y1 - 2019
SN - 1422-0067
UR - http://hdl.handle.net/11268/10787
AB - Unspecific peroxygenases (UPOs) are highly promiscuous biocatalyst with self-sufficient mono(per)oxygenase activity. A laboratory-evolved UPO secreted by yeast was covalently immobilized in activated carriers through one-point attachment. In order to maintain the desired orientation without compromising the enzyme’s activity, the S221C mutation was introduced at the surface of the enzyme, enabling a single disulfide bridge to be established between the support and the protein. Fluorescence confocal microscopy demonstrated the homogeneous distribution of the enzyme, regardless of the chemical nature of the carrier. This immobilized biocatalyst was characterized biochemically opening an exciting avenue for research into applied synthetic chemistry.
KW - Técnicas de química sintética
KW - Investigación empírica
KW - Enzima
KW - Química
LA - eng
ER -