[Zurück]


Vorträge und Posterpräsentationen (mit Tagungsband-Eintrag):

H. Mansouri Khosravi, C. P. Goncalves, S. Feroz, A. Bommarius, F. Rudroff, M.D. Mihovilovic:
"Activity and Stability Improvement of Cyclohexanone Monooxygenase by Protein Engineering";
Hauptvortrag: Vienna young Scientists Symposium (VSS) 2019, Wien; 13.06.2019 - 14.06.2019; in: "Vienna Young Scientist Symposium", F. Rudroff (Hrg.); -, Wien (2019), ISBN: 978-3-9504017-9-0; S. 64 - 65.



Kurzfassung englisch:
Among the great number of flavin-dependent monooxygenases, Baeyer-Villiger monooxygenases
(BVMOs) have been studied most for their application as a biocatalyst. These interesting
biocatalysts are capable of oxidizing carbonyl atoms into the corresponding esters or lactones[1] and
performing heteroatom oxidation reactions, like sulfoxidations. BVMOs usually exhibit high
chemo-, regio- and/or enantioselectivity while converting a wide variety of substrates. The
prototype BVMO, cyclohexanone monooxygenase (CHMO) is a promising biocatalyst for
industrial reactions owing to its broad substrate spectrum and the excellent stereoselectivity.
However, the low stability of BVMOs in general and especially for CHMO is an obstacle for their
exploitation in industry. [2,3] This unmet need is the main objective of this study.

Erstellt aus der Publikationsdatenbank der Technischen Universität Wien.