Abstract
One of the prerequisites for the functional and structural characterisation of proteins is to obtain a sufficiently high amount of the protein sample. Recombinant protein expression systems are usually employed for the overproduction of proteins in cases where isolation from their native host is difficult. For each protein, a suitable expression system must be optimised to obtain the sample in a soluble, correctly folded conformation with high production yield. The recent discovery of psychrophilic yeasts and their potential in industrial applications have sparked interest in overexpression strategies for high-level expression of psychrophilic proteins. Here, we discuss some of the recent developments in the recombinant production of cold-adapted yeast proteins, particularly those from Glaciozyma antarctica PI12, in suitable heterologous hosts. Findings from our work, as well as from recent publications, are included.
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Md. Illias, R., Ramli, A.N.M., Low, K.O., Muhammad Mahadi, N., Abdul Murad, A.M., Rabu, A. (2014). Heterologous Expression of Proteins from Cold-Adapted Yeasts in Suitable Hosts: Methods and Applications. In: Buzzini, P., Margesin, R. (eds) Cold-adapted Yeasts. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-39681-6_22
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DOI: https://doi.org/10.1007/978-3-642-39681-6_22
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