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Research Article Open access CC BY 4.0

Strategies for the Engineering of Recombinant Protein and its High Level Expression

Fayqa Komal, Faiza Asghar

International Journal of Biochemistry Research & Review · pp. 1–10 · Published 19 Jul 2016

10.9734/IJBCRR/2016/26639

Abstract

A large number of proteins are efficiently produced by microbes. Protein engineering especially working with enzymes has become a very promising section of the biotechnology industry. Due to increasing demands of proteins, bioengineering strategies have been gaining importance to modify natural enzymes. Commercially, hundreds of proteins are produced, the production of recombinant proteins still constitutes a challenge in many cases. Most common protein engineering techniques include i) Directed evolution, ii) Site-directed mutagenesis, iii) Truncation, iv) Terminal fusion. After engineering the desired protein, there is another great challenge to get the high level expression and solubility of the proteins. Four levels of strategies can be used to increase the expression and solubility of recombinant proteins; (1) vector selection, (2) host selection, (3) fermentation optimization and (4) codon optimization. Here we present the latest methods of protein engineering and molecular expression of industrially important enzymes and to get good quality of recombinant proteins. In this article, we have reviewed the different approaches, common problems, their solutions and also covered pros and cons of many of the latest used techniques in this ever-growing field.

Recombinant proteins directed evolution site directed mutagenesis truncation terminal fusion vector selection host selection codon optimization

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