Production and secretion dynamics of prokaryotic Penicillin G acylase in Pichia pastoris.

ABSTRACT: To take full advantage of recombinant Pichia pastoris (Komagataella phaffii) as a production system for heterologous proteins, the complex protein secretory process should be understood and optimised by circumventing bottlenecks. Typically, little or no attention has been paid to the fate of newly synthesised protein inside the cell, or its passage through the secretory pathway, and only the secreted product is measured. However, the system's productivity (i.e. specific production rate q_p), includes productivity of secreted (q_p,extra) plus intracellularly accumulated (q_p,intra) protein. In bioreactor cultivations with P. pastoris producing penicillin G acylase, we studied the dynamics of product formation, i.e. both the specific product secretion (q_p,e

SUBMITTER: Borcinova M 

PROVIDER: S-EPMC7306039 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature