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- W1502252160 abstract "α-Peptide, a portion of Escherichia coli β-galactosidase, was cloned downstream of the yeast α-factor promoter and the signal peptide by one of the authors. In this study, we utilized recombinant yeast cells, transformed the α-peptide secretion vector and attempted continuous production of α-peptide as a model of foreign peptide production. The continuous production of α-peptide was performed by using immobilized recombinant yeast cells on a column reactor, after characterizing the secretion, using minimal and complex medium. Utilizing minimal medium, with a productivity of 100 000 U h−1 l−1, α-peptide was continuously produced for more than 200 h. We then attempted to improve the productivity of α-peptide by alternating minimal and complex medium. Utilizing this medium changing method, 1.4 times higher α-peptide was produced during 150 h of operation compared with that achieved only by feeding minimal medium." @default.
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- W1502252160 date "1988-06-01" @default.
- W1502252160 modified "2023-09-24" @default.
- W1502252160 title "Continuous production of α-peptide using immobilized recombinant yeast cells" @default.
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- W1502252160 doi "https://doi.org/10.1016/0168-1656(88)90073-9" @default.
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