Proteins such as collagen, elastin, and silk play a crucial structure-forming role in various tissues and animal architecture such as spider webs. The unique properties of these proteins have sparked the interest of material scientists, who designed mimics and produced them in genetically modified organisms. The most commonly used production system for these so-called protein-based polymers is the bacterium Escherichia coli. In this thesis, we explored the use of an alternative platform, namely the yeast Pichia pastoris (Komagataella phafii). We genetically modified this yeast so that it produced mimics of collagen, gelatin, silk, or various combinations thereof. The proteins were secreted by the yeast into the growth medium at g/L levels. The basic physicochemical properties of the polymers were studied, which revealed interesting characteristics. Some of these polymers show promise for further development towards biomedical applications such as tissue engineering and controlled drug release.