Soluble recombinant protein production in Pseudoalteromonas haloplanktis TAC125

Solubility/activity issues are often experienced when immunoglobulin fragments are produced in conventional microbial cell factories. Although several experimental approaches have been followed to solve, or at least minimize, the accumulation of the recombinant proteins into insoluble aggregates, so...

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Bibliographic Details
Main Authors: Giuliani, Maria, PARRILLI, ERMENEGILDA, Sannino, Filomena, Apuzzo, Gennaro, MARINO, GENNARO, TUTINO, MARIA LUISA
Other Authors: Elena Garcìa-Fruitòs, Parrilli, Ermenegilda, Marino, Gennaro, Tutino, MARIA LUISA
Format: Book Part
Language:English
Published: Humana Press 2015
Subjects:
Batch fermentation
LIV medium
Pseudoalteromonas haloplanktis TAC125
Psychrophilic gene expression system
VHHD6.1
Antarctic
Antarc*
Online Access:http://hdl.handle.net/11588/612495
https://doi.org/10.1007/978-1-4939-2205-5_13
Description
Summary:Solubility/activity issues are often experienced when immunoglobulin fragments are produced in conventional microbial cell factories. Although several experimental approaches have been followed to solve, or at least minimize, the accumulation of the recombinant proteins into insoluble aggregates, sometimes the only alternative strategy is changing the protein production platform. In this chapter we describe the use of Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 as host of choice for the production of the heavy-chain antibody fragment VHHD6.1. Combining the use of a regulated psychrophilic gene expression system with an optimized fermentation process in defined growth medium, we obtained the recombinant VHHD6.1 in fully soluble form and correctly translocated into host periplasmic space.

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