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김용환

Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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Functional expression of Coprinus cinereus peroxidase in Pichia pastoris

Author(s)
Kim, Su JinLee, Jeong AhWon, KeehoonKim, Yong HwanSong, Bong Keun
Issued Date
2009-07
DOI
10.1016/j.procbio.2009.03.004
URI
https://scholarworks.unist.ac.kr/handle/201301/20388
Fulltext
http://www.sciencedirect.com/science/article/pii/S1359511309000841
Citation
PROCESS BIOCHEMISTRY, v.44, no.7, pp.731 - 735
Abstract
A Coprinus cinereus peroxidase (CiP) was successfully expressed by the methylotrophic yeast Pichia pastoris. The 1095-bp gene encoding peroxidase from C cinereus was cloned with a highly inducible alcohol oxidase (AOX1) promoter and integrated into the genome of P. pastoris. The recombinant CiP (rCiP) fused with the alpha-mating factor pre-pro leader sequence derived from Saccharomyces cerevisiae accumulated neither inside the cell nor within the wall, and were efficiently secreted into the Culture medium. SDS-PAGE and immunoblot analysis revealed that the rCiP was not hyper-glycosylated and its alpha-factor signal sequence was correctly processed. It was also found that the kinetic properties of rCiP were similar to those of native CiP. In order to produce large amounts of rCiP, the high cell density cultivation of recombinant P. pastoris was carried out in a fermentor with fed-batch mode. The peroxidase activity obtained in a 51 fermentor Cultivation became about 6 times (1200 U/ml) higher than that in shake-flask cultures (200 U/ml).
Publisher
ELSEVIER SCI LTD
ISSN
1359-5113

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