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Optimal Chemostat Cascades for Periplasmic Protein Production
Author(s) -
Davis Robert H.,
Ramirez W. Fred,
Chatterjee Ashish
Publication year - 1990
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00006a005
Subject(s) - chemostat , periplasmic space , yeast , saccharomyces cerevisiae , secretion , cascade , biology , productivity , steady state (chemistry) , protein biosynthesis , production (economics) , microbiology and biotechnology , secretory protein , biochemistry , chemistry , gene , genetics , escherichia coli , chromatography , bacteria , macroeconomics , economics
This theoretical work predicts the optimal system design for the steady‐state production of secreted protein in a chemostat cascade, using bakers' yeast (Saccharomyces cerevisiae) as the host organism. The protein of interest, mutant invertase, is secreted to the periplasmic space instead of the culture medium on account of its large size. This work uses the secretion model developed and tested by Park and Ramirez (1988). It is shown that the highest productivity is achieved when the chemostat cascade contains two stages, although the improvement over the single‐stage productivity is small. When no recycle is used, the advantage of two stages results from the tradeoff between maximizing the cell concentration and maximizing the rate of protein production per cell. When recycle is used, the cell concentration and protein productivity are increased, and the advantage of two stages results from the tradeoff between maximizing the specific protein production rate and maximizing the specific protein secretion rate. Cascades with three stages were also investigated, but these were found to have no improvement over the corresponding two‐stage cascades.