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박성훈

Park, Sunghoon
Biochemical Engineering Lab.
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Production of human caseinomacropeptide in recombinant Saccharomyces cerevisiae and Pichia pastoris

Author(s)
Kim, Yu-JinOh, You-KwanKang, WhankooLee, Eun YeolPark, Sunghoon
Issued Date
2005-09
DOI
10.1007/s10295-005-0010-2
URI
https://scholarworks.unist.ac.kr/handle/201301/25375
Fulltext
https://link.springer.com/article/10.1007%2Fs10295-005-0010-2
Citation
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, v.32, no.9, pp.402 - 408
Abstract
Caseinomacropeptide is a polypeptide of 64 amino acid residues (106-169) derived from the C-terminal part of the mammalian milk k-casein. This macropeptide has various biological activities and is used as a functional food ingredient as well as a pharmaceutical compound. The gene encoding the human caseinomacropeptide (hCMP) was synthesized and expressed with an alpha-factor secretion signal in the two yeast strains, Saccharomyces cerevisiae and Pichia pastoris. The complete polypeptide of the recombinant hCMP was produced and secreted in a culture medium by both the strains, but the highest production was observed in S. cerevisiae with a galactose-inducible promoter. In a fed-batch bioreactor culture, 2.5 g/l of the recombinant hCMP was obtained from the S. cerevisiae at 97 h.
Publisher
SPRINGER HEIDELBERG
ISSN
1367-5435
Keyword (Author)
caseinomacropeptiderecombinant yeastsecretionpromoterfed-batch
Keyword
HUMAN LIPOCORTIN-IFEEDING STRATEGYGAL10 PROMOTEREXPRESSIONPURIFICATIONSEQUENCESYEASTS

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