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Maximizing recombinant human serum albumin production in a Mut s Pichia pastoris strain
Author(s) -
Mallem Muralidhar,
Warburton Shan,
Li Fang,
Shandil Ishaan,
Nylen Adam,
Kim Sehoon,
Jiang Youwei,
Meehl Michael,
d'Anjou Marc,
Stadheim Terrance A.,
Choi ByungKwon
Publication year - 2014
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.1990
Subject(s) - pichia pastoris , recombinant dna , titer , human serum albumin , fermentation , strain (injury) , pichia , chemistry , methanol , albumin , biochemistry , biology , immunology , antibody , gene , organic chemistry , anatomy
Human serum albumin (HSA) is a cysteine rich molecule that is most abundant in human blood plasma. To remain viable in the market due to lower marketing costs for HSA, it is important to produce a large quantity in an economical manner by recombinant technology. The objective of this study was to maximize recombinant HSA (rHSA) production using a Mut s Pichia pastoris strain by fermentation process optimization. We evaluated the impact of process parameters on the production of rHSA, including induction cell density (wet cell weight, g/L) and the control of specific growth rate at induction. In this study, we demonstrated that induction cell density is a critical factor for high level production of rHSA under controlled specific growth rate. We observed higher specific productivities at higher induction cell densities (285 g/L) and at lower specific growth rates (0.0022–0.0024/h) during methanol induction phase, and achieved the broth titer of rHSA up to 10 g/L. The temperature shift from 24 to 28 o C was effective to control the specific growth rate at low level (≤0.0024/h) during methanol induction phase while maintaining high specific productivity [0.0908 mg rHSA /(g wcw h)]. © 2014 American Institute of Chemical Engineers Biotechnol. Prog ., 30:1488–1496, 2014