Collagen is a structural protein characterized by its triple-helical arrangement,
which imparts remarkable tensile strength and stability. These properties
make collagen highly valuable in diverse applications, ranging from cosmetic
formulations to advanced biomaterials for tissue engineering and regenerative
medicine. Traditionally, collagen is extracted from animal sources such as bovine
and porcine tissues. However, these sources present ethical concerns, risk of
zoonotic disease transmission, and potential contamination with heavy metals
or pathogens. To address these challenges, we have developed a novel microbial
platform for producing functional collagen-like proteins.
Streptococcal collagen-like protein (Scl2), derived from bacteria, mimics the
structural and mechanical properties of mammalian collagen without requiring
complex post-translational modifications such as hydroxyproline formation. This
feature makes Scl2 an attractive candidate for scalable production while retaining
the functional qualities necessary for biomaterial applications. In our study,
we successfully employed Gibson assembly for plasmid construction, followed
by lithium acetate-mediated transformation into Saccharomyces cerevisiae.
The expression and integrity of Scl2 were confirmed through DNA and protein
gel electrophoresis. Furthermore, we performed comparative extraction of
mammalian collagen to benchmark its physicochemical properties and evaluate
its potential incorporation into hydrogel formulations. Our results demonstrate
that microbial-derived Scl2 can serve as a sustainable and ethically responsible
alternative to animal collagen, offering comparable structural performance and
high potential for biomedical and industrial applications.