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Pichia pastoris secretes recombinant proteins less efficiently than Chinese hamster ovary cells but allows higher space‐time yields for less complex proteins
Author(s) -
Maccani Andreas,
Landes Nils,
Stadlmayr Gerhard,
Maresch Daniel,
Leitner Christian,
Maurer Michael,
Gasser Brigitte,
Ernst Wolfgang,
Kunert Renate,
Mattanovich Diethard
Publication year - 2014
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201300305
Subject(s) - pichia pastoris , chinese hamster ovary cell , recombinant dna , pichia , microbiology and biotechnology , hamster , chemistry , biochemistry , biology , receptor , gene
Chinese hamster ovary (CHO) cells are currently the workhorse of the biopharmaceutical industry. However, yeasts such as Pichia pastoris are about to enter this field. To compare their capability for recombinant protein secretion, P. pastoris strains and CHO cell lines producing human serum albumin (HSA) and the 3D6 single chain Fv‐Fc anti‐HIV‐1 antibody (3D6scFv‐Fc) were cultivated in comparable fed batch processes. In P. pastoris , the mean biomass‐specific secretion rate ( q p ) was 40‐fold lower for 3D6scFv‐Fc compared to HSA. On the contrary, q p was similar for both proteins in CHO cells. When comparing both organisms, the mean q p of the CHO cell lines was 1011‐fold higher for 3D6scFv‐Fc and 26‐fold higher for HSA. Due to the low q p of the 3D6scFv‐Fc producing strain, the space‐time yield (STY) was 9.6‐fold lower for P. pastoris . In contrast, the STY of the HSA producer was 9.2‐fold higher compared to CHO cells because of the shorter process time and higher biomass density. The results indicate that the protein secretion machinery of P. pastoris is much less efficient and the secretion rate strongly depends on the complexity of the recombinant protein. However, process efficiency of the yeast system allows higher STYs for less complex proteins.