Abstract
Recombinant protein production represents a multibillion-dollar market. Therefore, it constitutes an important research field both in academia and industry. The use of yeast as a cell factory presents several advantages such as ease of genetic manipulation, growth at high cell density, and the possibility of post-translational modifications. Yarrowia lipolytica is considered as one of the most attractive hosts due to its ability to metabolize raw substrate, to express genes at a high level, and to secrete protein in large amounts. In recent years, several reviews have been dedicated to genetic tools developed for this purpose. Though the construction of efficient cell factories for recombinant protein synthesis is important, the development of an efficient process for recombinant protein production in a bioreactor constitutes an equally vital aspect. Indeed, a sports car cannot drive fast on a gravel road. The aim of this review is to provide a comprehensive snapshot of process tools to consider for recombinant protein production in bioreactor using Y. lipolytica as a cell factory, in order to facilitate the decision-making for future strain and process engineering.
Highlights
Recombinant protein production represents a multibillion-dollar market [1,2]
The aim of the present review is to provide a comprehensive snapshot of the already available and future molecular and process tools to consider for recombinant protein production in bioreactor using Y. lipolytica as a cell factory, in order to facilitate decision-making for future strain and process engineering
Aside from overexpressed endogenous genes, reactor-scale production by Y. lipolytica has mainly focused on recombinant proteins from fungal origin, some examples of viral [6], bacteria [7,8,9,10,11], vegetal [12,13,14,15], or mammalian [16,17,18,19,20] proteins have been reported over the years
Summary
Recombinant protein production represents a multibillion-dollar market [1,2]. It has been developed as a safer and cost-effective alternative to the extraction of proteins from natural sources. Yeasts combine the characteristics of the former (i.e., simplicity of growth and genetic engineering) and the latter (i.e., protein folding and assembly, post-translational modifications) In this regard, Yarrowia lipolytica stands out as an advantageous host system. Y. lipolytica secretes large amounts of hydrolases, mainly lipases and proteases, to retrieve nutrients necessary to sustain its growth. This goes together with a very efficient secretory pathway [4]. The aim of the present review is to provide a comprehensive snapshot of the already available and future molecular and process tools to consider for recombinant protein production in bioreactor using Y. lipolytica as a cell factory, in order to facilitate decision-making for future strain and process engineering
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