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Ioannis V. Pavlidis

Researcher at University of Crete

Publications -  57
Citations -  1718

Ioannis V. Pavlidis is an academic researcher from University of Crete. The author has contributed to research in topics: Immobilized enzyme & Catalysis. The author has an hindex of 19, co-authored 52 publications receiving 1405 citations. Previous affiliations of Ioannis V. Pavlidis include University of Greifswald & University of Ioannina.

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Identification of (S)-selective transaminases for the asymmetric synthesis of bulky chiral amines

TL;DR: The creation of highly active and stereoselective transaminases starting from fold class I are reported and can be engineered into other protein scaffolds with sequence identities as low as 70%, and should have a broad impact in the field of biocatalytic synthesis and enzyme engineering.
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Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials.

TL;DR: The enhanced catalytic behavior observed for most of the hydrolases covalently immobilized on amine-functionalized CNTs indicate that these functionalized nanomaterials are suitable for the development of efficient nanobiocatalytic systems.
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Graphene-based nanobiocatalytic systems: recent advances and future prospects

TL;DR: The current advances in research on graphene-based nanomaterials used as novel scaffolds to build robust nanobiocatalytic systems are presented and the implications of such interactions along with future prospects and possible challenges are discussed.
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Lipases in water-in-ionic liquid microemulsions: Structural and activity studies

TL;DR: Conformational studies via Fourier transform-infrared (FT-IR) and circular dichroism (CD) spectroscopy indicated that lipases entrapped in w/IL microemulsions in most cases retain their native structure or adapt a more rigid structure compared to other microheterogeneous media, which correlated well with the stability results.
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Lipase immobilization on smectite nanoclays: Characterization and application to the epoxidation of alpha-pinene

TL;DR: Structural and biochemical characterization have revealed that the hydrophobic microenvironment created by the organo-modified clays induces minor changes on the secondary structure of the enzyme, resulting in enhanced catalytic behaviour in hydrophilic media.