Expression of Recombinant Human Collagens in Pichia Pastoris

As the main protein family in the extracellular matrix, collagen plays an important role in diverse biological functions. These collagens are mainly isolated from animal tissues, and the risk of animal-derived contaminating pathogens and the difficulties of preparation with the same chemical composition must be considered. The use of genetically engineered microorganisms is a cost-effective and scalable technology for the production of recombinant human collagen. In addition, the methylotrophic yeast Pichia Pastoris is considered to be an excellent host for the production of heterologous proteins.

Most recombinant systems currently used for mass production of recombinant proteins cannot be applied to the production of recombinant human collagens because they do not have prolyl 4-hydroxylase (4-PH) activity. Methods have been developed for producing the three major fibril-forming human collagens, types I, II and III, in the methylotrophic yeast Pichia pastoris ^[1]. These methods are based on the co-expression of procollagen polypeptide chains with the α- and β-subunits of proline 4-hydroxylase. Triple-helix types I, -II, and -III procollagens have been found to accumulate predominantly in the endoplasmic reticulum of yeast cells and could be purified from cell lysates by procedures including pepsin treatment, conversion of procollagen to collagen, and digestion of most of the non-collagenous proteins.

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