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Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase.


ABSTRACT: 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.

SUBMITTER: Molina-Espeja P 

PROVIDER: S-EPMC6480235 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase.

Molina-Espeja Patricia P   Santos-Moriano Paloma P   García-Ruiz Eva E   Ballesteros Antonio A   Plou Francisco J FJ   Alcalde Miguel M  

International journal of molecular sciences 20190402 7


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 confo  ...[more]

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