Functional expression of recombinant goat chymosin in Pichia pastoris bioreactor cultures: A commercially viable alternate

摘要: Abstract Recombinant goat chymosin (RGC), a promising alternate of bovine/calf chymosin, has better catalytic, proteolytic and thermostable characteristics. Limited information exists about its expression in different hosts. Pichia pastoris (P. pastoris) ability to grow very high cell densities improved protein production been demonstrated scale up studies. A modified methanol feeding strategy based on flask level optimizations was successfully used for expressing the prochymosin recombinant methylotrophic yeast P. Mut+ bioreactor cultures. Additionally, comparative analysis RGC versus cultures performed. Bioreactor yielded an approximate 8 times increase density compared prior induction 24% also recorded. Functional characterization that enzyme produced even at early stages found be correctly folded, intact functional. The preparation 42.4% residual activity 60 °C retained 69% pH 6.5. An RGC, which can act as lead industrially viable preparation, is outlined present study.