With strong potential for being an expression system for protein production, as well as being a model organism for genetic study, Komagataella phaffii has become important for biological research and biotech applications.

[10] The growth rate of its colonies can vary by a large range, from near to 0 to a doubling time of one hour, which is suitable for industrial processes.

Like other widely used yeast models, it has relatively short life span and fast regeneration time.

Moreover, some inexpensive culture media have been designed, so that Komagataella can grow quickly on them, with high cell density.

The complete genomic data allows scientists to identify homologous proteins and evolutionary relationships between other yeast species and Komagataella.

The two yeast genera; Pichia (sensu lato) and Saccharomyces, have similar growth conditions and tolerances; thus, the culture of Komagataella can be adopted by labs without many modifications.

[15] Moreover, unlike S. cerevisiae, Komagataella has the ability to functionally process proteins with large molecular weight, which is useful in a translational host.

[18] In the last decade, Komagataella was engineered to build expression system platforms, which is a typical application for a standard experimental model organism, as described below.

[19] Some common variants possess a mutation in the HIS4 gene, leading to the selection of cells which are transformed successfully with expression vectors.

[26][27] In standard molecular biology research, the bacterium Escherichia coli is the most frequently used organism for expression system, to produce heterologous proteins, due to its features of fast growth rate, high protein production rate, as well as undemanding growth conditions.

[29] The well-studied Saccharomyces cerevisiae is also used as an expression system with similar advantages over E. coli as Komagataella.

Generally, cell lines from multicellular organisms require complex and expensive types of media, including amino acids, vitamins, as well as other growth factors.

At the beginning, one drawback of this protein expression system is the over-glycosylation with high density of mannose structure, which is a potential cause of immunogenicity.