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Scientific Overview of Pichia Pastoris Expression System

Proteins are ideal for various industries, including biopharmaceuticals, enzymes, and agriculture. Medicine, diagnostics, food, nutrition, detergents, textiles, leather, paper, pulp, polymers, and plastics all benefit from the products of these sectors. The potential scope for these professions has drastically altered recombinant DNA technology since the 1970s.

Bacteria, yeast, filamentous fungi, insect cells, mammalian cells, transgenic animals, and transgenic plants create recombinant proteins. E. coli produces 39 percent of recombinant proteins, CHO cells 35 percent, yeasts 15 percent, other mammalian systems 10 percent, and other bacteria and other systems 1 percent. Yeasts and molds produce more than half of all industrial enzymes, with bacteria accounting for 30%, mammals for 8%, and plants for 4%.

Proteins with a molecular weight greater than 100 kD are expressed in eukaryotic systems, while those with a molecular weight less than 30 kD are in prokaryotic systems. Bacterial cells are easy to use, have a fast generation period, and produce huge product yields at a low cost.

Like bacteria, yeasts, single-celled organisms that are easy to manage and maintain, also provide a eukaryotic environment, which is often necessary for creating big and complicated proteins.

Understanding The Pichia Pastoris Expression System

The Pichia pastoris expression system has become one of the most widely utilized. P. pastoris, together with E. coli, B. subtilis, S. cerevisiae, H. polymorpha, and Aspergillus and Trichoderma species, is now a well-established industrial platform for protein production.

Through homologous recombination, linear vectors are incorporated into the P. pastoris genome and can produce stable transformants.

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