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Autodisplay of enzymes—Molecular basis and perspectives

Paper ID Volume ID Publish Year Pages File Format Full-Text
23790 43473 2012 12 PDF Available
Title
Autodisplay of enzymes—Molecular basis and perspectives
Abstract

To display an enzyme on the surface of a living cell is an important step forward towards a broader use of biocatalysts. Enzymes immobilized on surfaces appeared to be more stable compared to free molecules. It is possible by standard techniques to let the bacterial cell (e.g. Escherichia coli) decorate its surface with the enzyme and produce it on high amounts with a minimum of costs and equipment. Moreover, these cells can be recovered and reused in several subsequent process cycles. Among other systems, autodisplay has some extra features that could overcome limitations in the industrial applications of enzymes. One major advantage of autodisplay is the motility of the anchoring domain. Enzyme subunits exposed at the cell surface having affinity to each other will spontaneously form dimers or multimers. Using autodisplay enzymes with prosthetic groups can be displayed, expanding the application of surface display to the industrial important P450 enzymes. Finally, up to 105–106 enzyme molecules can be displayed on a single cell. In the present review, we summarize recent achievements in the autodisplay of enzymes with particular attention to industrial needs and process development. Applications that will provide sustainable solutions towards a bio-based industry are discussed.

► A comprehensive review on the Autodisplay of enzymes in E. coli is presented. ► With particular attention to industrial needs and process development. ► Applications of whole cells displaying enzymes for sustainable solutions towards a bio-based industry are discussed.

Keywords
Autodisplay; Biocatalysis; Synthesis; Enzymes; Whole cells
First Page Preview
Autodisplay of enzymes—Molecular basis and perspectives
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 161, Issue 2, 15 October 2012, Pages 92–103
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering