Proteolysis of recombinant proteins in bioengineered plant cells
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Date
Authors
Pillay, Priyen
Schluter, Urte
Van Wyk, Stefan
Kunert, Karl J.
Vorster, Barend Juan
Journal Title
Journal ISSN
Volume Title
Publisher
Routledge
Abstract
Plants are increasingly used as alternative expression hosts for the
production of recombinant proteins offering many advantages
including higher biomass and the ability to perform posttranslational
modifications on complex proteins. Key challenges
for optimized accumulation of recombinant proteins in a plant
system still remain, including endogenous plant proteolytic
activity, which may severely compromise recombinant protein
stability. Several strategies have recently been applied to improve
protein stability by limiting protease action such as recombinant
protein production in various sub-cellular compartments or
application of protease inhibitors to limit protease action. A
short update on the current strategies applied is provided here,
with particular focus on sub-cellular sites previously selected
for recombinant protein production and the co-expression of
protease inhibitors to limit protease activity.
Description
Keywords
Recombinant protein production in plants, Protein stability, Proteases, Protease inhibitors
Sustainable Development Goals
Citation
Priyen Pillay, Urte Schlüter, Stefan van Wyk, Karl Josef Kunert & Barend Juan Vorster (2014) Proteolysis of recombinant proteins in bioengineered plant cells, Bioengineered, 5:1, 15-20, DOI: 10.4161/bioe.25158