Production of human caseinomacropeptide in recombinant Saccharomyces cerevisiae and Pichia pastoris |
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| Authors: | Yu-Jin Kim You-Kwan Oh Whankoo Kang Eun Yeol Lee Sunghoon Park |
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| Institution: | (1) Department of Chemical Engineering and Institute for Environmental Technology and Industry, Pusan National University, 30 Jangjeon-dong, Geumjeong-gu, Busan, 609-735, Republic of Korea;(2) Department of Chemical Engineering and Nano-Bio Technology, Hannam University, 133 Ojeong-dong, Daedeok-gu, Daejeon, 306-791, Republic of Korea;(3) Department of Food Science and Technology, Kyungsung University, 110-1 Daeyeon-dong, Nam-gu, Busan, 608-736, Republic of Korea |
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| 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 α-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. |
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| Keywords: | Caseinomacropeptide Recombinant yeast Secretion Promoter Fed-batch |
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