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.
authors.affiliation: Institut für Pharmazeutische und Medizinische Chemie, Westfälische Wilhelms-Universität Münster, D-48149 Münster, Germany. joachim.jose@uni-muenster.de
authors.forename: Joachim
authors.initials: J
authors.lastname: Jose
authors.forename: Ruth Maria
authors.initials: RM
authors.lastname: Maas
authors.forename: Mark George
authors.initials: MG
authors.lastname: Teese
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D055162:Biocatalysis; D019149:Bioreactors; D001709:Biotechnology / Q000379:methods*; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000201:enzymology; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D004798:Enzymes; D004800:Enzymes, Immobilized; D008565:Membrane Proteins; D011994:Recombinant Proteins