Several different types of digestive proteinases were also highly expressed and included M16 peptidases, M14 carboxypeptidases, serine proteinases, and cysteine proteinases, which likely serve key roles in nitrogen extraction from plant or microbial cell wall proteins.
The detailed analysis of the P. pastoris plasma membrane is discussed in the light of cell biological features of this microorganism especially as a microbial cell factory for heterologous protein production.
Another technique for manufacturing bioactive peptides includes the expression of recombinant protein in the microbial cell followed by the hydrolysis of the fusion protein by microbial proteinase.
The cell surface display technique allows for the expression of target proteins or peptides on the microbial cell surface by fusing an appropriate protein as an anchoring motif.
Recent studies have indicated that AMPs can also inhibit the biosynthesis of microbial cell walls, nucleic acids, and proteins, and can inhibit the activity of certain microbial enzymes [19], [20], [21], [22].
The major targets in the microbial cell include surface-exposed adhesin proteins, cell wall polypeptides, and membrane-bound enzymes [ 44].
The display of heterologous proteins on the microbial cell surface by means of recombinant DNA biotechnologies has emerged as a novel approach for bioremediation of contaminated sites.
Hansenula polymorpha DL1 is a methylotrophic yeast, widely used in fundamental studies of methanol metabolism, peroxisome biogenesis and function, and also as a microbial cell factory for production of recombinant proteins and metabolic engineering towards the goal of high temperature ethanol production.
The yeast Pichia pastoris GS115 is a widely used microbial cell factory for the production of heterologous protein.
It is a long time since Escherichia coli (E. coli) was developed as an ideal microbial cell factory for the production of recombinant proteins.
