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Marine mussels adhere to substrates within the intertidal zone by means of a bundle of threads called the mussel byssus which contains several collagen-like proteins responsible for the mechanical properties of the fibers. Here, we demonstrate the biotechnological production of one of three identified byssus collagens, preColD, from Mytilus galloprovincialis using Pichia pastoris as the expression host. Previously detected structural features of natural preColD, such as collagen triple helix formation, could also be detected in the recombinant preColD, even in the absence of hydroxylation of proline or tyrosine residues.

Biotechnological production of the mussel byssus derived collagen preColD