Abstract: The present invention provides a fermentation process for improving the production level of a recombinant human collagen. The process comprises inoculating a sterilized fermentation medium with a Pichia yeast solution, then performing fermentation culturing for 14-18 hrs, adding methanol to induce the expression, upon which sodium pyruvate is added to the fermentation medium, wherein the amount of the sodium pyruvate added is 0.01-10 g/L. In the fermentation process of the present invention, the sodium pyruvate is added in the methanol-induced expression stage, so that the biosynthesis rate of the recombinant human collagen is improved; and a continuous feed-batch mode is adopted, so that the biosynthesis rate of the recombinant human collagen is further improved, and the fermentation time is shortened. Meanwhile, the expression level of the recombinant human collagen is increased, the fermentation level is increased by more than 20%, and the production cost is reduced.

Abstract: The present invention discloses a fermentation process with a Pichia yeast expressing a recombinant protein, in which Pichia pastoris is used as a fungal strain. The process comprises performing primary seed culturing to reach a fungal concentration of 20±2 g/L; then performing secondary seed culturing to reach a fungal concentration of 120±10 g/L; next proceeding to a glycerol culturing stage, wherein the amount of glycerol added in the glycerol culturing stage is 60-70 g/L; and then proceeding to a methanol-induced stage for 120±8 h after the dissolved oxygen quickly reaches a relatively stable state, to complete the fermentation process. In the present invention, a glycerol fed-batch addition stage in existing processes is omitted, and the process proceeds to a next stage as soon as glycerol is completely consumed, with no need to prepare sterilized glycerol for fluidic addition. As such, the glycerin sterilizer is omitted, the consumption of energy and resource and the waste of glycerin are reduced.

Abstract: The present invention discloses a fermentation process with a Pichia yeast expressing a recombinant protein, in which Pichia pastoris is used as a fungal strain. The process comprises performing primary seed culturing to reach a fungal concentration of 20±2 g/L; then performing secondary seed culturing to reach a fungal concentration of 120±10 g/L; next proceeding to a glycerol culturing stage, wherein the amount of glycerol added in the glycerol culturing stage is 60-70 g/L; and then proceeding to a methanol-induced stage for 120±8 h after the dissolved oxygen quickly reaches a relatively stable state, to complete the fermentation process. In the present invention, a glycerol fed-batch addition stage in existing processes is omitted, and the process proceeds to a next stage as soon as glycerol is completely consumed, with no need to prepare sterilized glycerol for fluidic addition. As such, the glycerin sterilizer is omitted, the consumption of energy and resource and the waste of glycerin are reduced.

Abstract: The present invention provides a fermentation process for improving the production level of a recombinant human collagen. The process comprises inoculating a sterilized fermentation medium with a Pichia yeast solution, then performing fermentation culturing for 14-18 hrs, adding methanol to induce the expression, upon which sodium pyruvate is added to the fermentation medium, wherein the amount of the sodium pyruvate added is 0.01-10 g/L. In the fermentation process of the present invention, the sodium pyruvate is added in the methanol-induced expression stage, so that the biosynthesis rate of the recombinant human collagen is improved; and a continuous feed-batch mode is adopted, so that the biosynthesis rate of the recombinant human collagen is further improved, and the fermentation time is shortened. Meanwhile, the expression level of the recombinant human collagen is increased, the fermentation level is increased by more than 20%, and the production cost is reduced.