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Volume 2, Issue 3 And 4 (3-2019)                   زیست شناسی 2019, 2(3 And 4): 121-130 | Back to browse issues page

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Fabriki Ourang S. Strategies required for expression and production of recombinant proteins in plants and their purification. زیست شناسی. 2019; 2 (3 and 4) :121-130
URL: http://ijbio.ir/article-1-34-en.html
Imam Khomeini International University, Imam Khomeini International University, Qazvin, Iran , s.ourang910@gmail.com
Abstract:   (1012 Views)

Engineered plants as bioreactors for production of heterologous proteins are appropriate replacement for conventional expression systems such as mammalian cell culture and transgenic animals. For efficient production of recombinant proteins, the type of host species is very important and its choice depends on the type of recombinant proteins, plant life cycle and its performance, and maintenance or production costs. The most important benefits of plant-based expression systems could be included: cost effective of the plant systems, no contamination of recombinant proteins derived from plants with human pathogenic microorganisms due to host-less of plants to human pathogens, easy and low cost of extraction and purification of proteins, more post-translational changes required for the stability and activity of protein by plants. For development of plant-based production of recombinant proteins, optimization of protein expression level is essential. In this regard; various factors controlling the expression of target gene at levels of transcription, translation, post-translational modifications and recombinant protein accumulation are involved. On the other hand, lower amounts of expressed recombinant proteins are serious problem limiting commercial exploitation of plants bioreactors. Thus improving the accumulation of recombinant proteins in transgenic plants is an important factor in the desirability of an expression system. In this regard, the accession of signals in C-terminal of target proteins leads to increased retention and accumulation of proteins in the endoplasmic reticulum. After production of recombinant proteins, the use of affinity tag for purification of proteins are very effective and useful, so protein purification will possible without prior notification of their biochemical properties.

     
Type of Study: Review Paper |
Received: 2017/01/22 | Accepted: 2017/07/10 | Published: 2019/07/24

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