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• W2078272616 abstract "A recombinant puroindoline-a (rPIN-a) was produced using the methylotrophic yeast Pichia pastoris.In fed-batch culture, the production of rPIN-a decreased after 24 h of methanol induction. Most of the rPIN-a was not soluble in the culture medium remaining bound to the cell walls. Soluble and membrane-bound rPIN-a were quantified by ELISA after Triton X-114 phase partitioning. In order to improve the production of rPIN-a, the influence of pH, specific growth rate and the addition of TX-114 was tested on two independent continuous cultures. The production of rPIN-a was improved when continuous culture was carried out at 29 degrees C under acid conditions (pH 5) with a low dilution rate (D=0.025 h(-1)). The addition of 0.01% TX-114 to the medium inverted the ratio between the secreted and the membrane-bound rPIN-a.When a continuous culture was carried out under optimized conditions, the rPIN-a production yield was increased 10-fold to 14 mg l(-1) and 80% of the rPIN-a was soluble.This study would be helpful to optimize the expression of other membrane-bound proteins in P. pastoris." @default.
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• W2078272616 date "2001-03-02" @default.
• W2078272616 modified "2023-09-24" @default.
• W2078272616 title "Optimization of the wheat puroindoline-a production in Pichia pastoris" @default.
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• W2078272616 doi "https://doi.org/10.1046/j.1365-2672.2001.01259.x" @default.
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