@conference{
author = "Balaz, Ana Marija and Popov, Neda and Prodanović, Olivera and Ostafe, Raluca and Fischer, Rainer and Prodanović, Radivoje",
year = "2019",
abstract = "Phanerochaete chrysosporium is a white rot fungi and it has been known to secrete
flavocytochrome enzyme cellobiose dehydrogenase (CDH, EC 1.1.99.18) which contains
two domains, a flavine domain and cytochrome domain. Flavine domain contains FAD as
prostetic group and its catalytically active domain, whereas cytochrome domain serves as
electrone acceptor. Cellobiose and lactose, as well as other β – 1,4 – linked disaccharides
and oligosaccharides, have been oxidized by the cellobiose dehydrogenase to their
corresponding lactones. CDH can be used for constructing biosensors and therefore
directed evolution has been used to produce more active and stable variants of the enzyme.
Wild type CDH enzyme was expressed in S.cerevisiae INVSc1 cells and used for creation
of saturation mutagenesis libraries at M65, M685 and M738 and screening for increased
oxidative stability. More stable mutants that were found were recloned into Pichia pastoris
KM71H strain for higher expression yield. They were afterwards, expressed in Pichia,
purified and kineticaly characterized.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "The 9th conference of the Serbian Biochemical Society: Diversity in Biochemistry",
title = "Characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase mutants with increased oxidative stability from Pichia pastoris KM71H strain",
pages = "75-74",
url = "https://hdl.handle.net/21.15107/rcub_rimsi_3043"
}