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Frontiers of Chemical Science and Engineering

ISSN 2095-0179

ISSN 2095-0187(Online)

CN 11-5981/TQ

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Front. Chem. Sci. Eng.    2017, Vol. 11 Issue (1) : 46-57    https://doi.org/10.1007/s11705-017-1609-3
REVIEW ARTICLE
Cell surface protein engineering for high-performance whole-cell catalysts
Hajime Nakatani,Katsutoshi Hori()
Department of Biotechnology, Graduate School of Engineering, Nagoya University, Nagoya 464-8603, Japan
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Abstract

Cell surface protein engineering facilitated by accumulation of information on genome and protein structure involves heterologous production and modification of cell surface proteins using genetic engineering, and is important for the development of high-performance whole-cell catalysts. In this field, cell surface display is a major technology by exposing target proteins, such as enzymes, on the cell surface using a carrier protein. The target proteins are fused to the carrier proteins that transport and tether them to the cell surface, as well as to a secretion signal. This paper reviews cell surface display systems for prokaryotic and eukaryotic cells from the perspective of carrier proteins, which determine the number of displayed molecules, and the localization, size, and direction (N- or C-terminal anchoring) of the passengers. We also discuss advanced methods for displaying multiple enzymes and a new method for the immobilization of whole-cell catalysts using adhesive surface proteins.
Keywords cell surface engineering      surface display      whole-cell catalysts      bioprocess     
Corresponding Author(s): Katsutoshi Hori   
Online First Date: 13 February 2017    Issue Date: 17 March 2017
 Cite this article:   
Hajime Nakatani,Katsutoshi Hori. Cell surface protein engineering for high-performance whole-cell catalysts[J]. Front. Chem. Sci. Eng., 2017, 11(1): 46-57.
 URL:  
https://academic.hep.com.cn/fcse/EN/10.1007/s11705-017-1609-3
https://academic.hep.com.cn/fcse/EN/Y2017/V11/I1/46
Fig.1  Major microbial cell surface display systems. (A) Gram-negative and (B) Gram-positive bacterial cell surface display systems, and (C) yeast surface display systems. Abbreviations: Lpp, lipoprotein peptides; OmpA, outer membrane protein A; INPs, ice nucleation proteins; SpA, Staphylococcal protein A; FnBPB, fibronecti n-binding protein B; SrtA, sortase A
Fig.2  Cell surface display of multiple proteins. (A) Co-display of multiple enzymes on Gram-negative bacteria and (B) multiple protein display on the yeast cell surface via a scaffoldin-based system
Carrier protein Host Passenger protein Application Ref.
Prokaryotes / Single protein display
Lpp-OmpA Escherichia coli Cex* or CBDCex** from Cellulomonas fimi Degradation of cellulose 24
Lpp-OmpA E. coli DH10B PbrR*** from Cupriavidus metallidurans CH34 Lead ion adsorption 25
Lpp-OmpA E. coli Thermomyces lanuginosus DSM 5826 xylanase (XynA) Oligosaccharide synthesis 28
Lpp-OmpA E. coli Methyl parathion hydrolase (MPH)-GFP fusion Bioremediation 26
INPs E. coliMC1061, MC4100 Alditol oxidase from Streptomyces coelicolor Biochemical conversion 34
INPs E. coli DH5α Mammalian NADPH-cytochrome P450 oxidoreductase Biochemical conversion/bioremediation 36
INPs E. coli DH5α Organophosphorus hydrolase (OPH) Bioremediation 88
AIDA-I E. coli UT5600, UT5600 (DE3) Sorbitol dehydrogenase from Rhodobacter sphaeroides Bioconversion 42
AIDA-I E. coliBL21 (DE3) Esterase (ApeE) from Salmonella enterica Typhimurium Screening of hydrolases 44
AIDA-I E. coli UT5600 OPH Bioremediation 45
AIDA-I / INPs / Lpp-OmpA E. coliJM109, XL1-Blue, BL21(DE3), UT5600 MPH Bioremediation 89
EstA E. coli71-18, BL21(DE3) Bacillus subtilis lipase LipA; Fusarium solani pisi cutinase; Serratia marcescens lipase Screening of lipase variant 46
MATE**** system Pseudomonas putida KT2440 Cellulases CelK, CelA and β-glucosidase BglA from Clostridium thermocellum Degradation of cellulose 51
Prokaryotes / Multiple protein display
Lpp-OmpA / INPs E. coli XL1-Blue MPH-GFP fusion protein; OPH Bioremediation 87
Eukaryotes / Single protein display
a-Agglutinin (Aga1p / Aga2p) Saccharomyces cerevisiaeEBY100 Xylanase (Xyn) from Paenibacillus polymyxa PPL-3 Removal of hemicellulose from pulp 64
a-Agglutinin (Aga1p / Aga2p) S. cerevisiae EBY100 Laccases from Trametes versicolor Bioremediation 67
a-Agglutinin (Aga1p / Aga3p) S. cerevisiae EBY100 Linoleic acid isomerase from Propionibacterium acnes Biochemical conversion 68
α-Agglutinin (Agα1) S. cerevisiaeYF207 Rhizopus oryzae glucoamylase Bioethanol production 66
Flocculation protein (Flo1) S. cerevisiaeATCC 60715 Rhizopus oryzae lipase with a pro sequence (ProROL) Biodiesel production 70
Flocculation protein (Flo2) Pichia pastoris Rhizomucor miehei lipase variant Biochemical conversion 71
Flocculation protein (Flo3) Pichia pastorisKM71 Yarrowia lipolytica AS 2.1216 lipase LiPY7 and LiPY8 Biochemical conversion 72
Flocculation protein (Flo9) / Pir1 Pichia pastoris Lipase B from Candida antarctica (LipB) Biochemical conversion 73
Proteins with internal repeats (Pir) Pichia pastorisGS115 Endoglucanase Bioconversion 81
Pir1 / Pir2 S. cerevisiaeYAT, YAB, YOB strains Human α-1,3-fucosyltansferase (FucT) Oligosaccharide synthesis 77
Pir4 S. cerevisiae Bacillus sp. BP-7 xylanase A Removal of hemicellulose from pulp 79
Pir1 / Pir3 / Pir4 S. cerevisiaeW303-1A, YSF123, YSF124 Fifty-one human glycosyltransferases Human oligosaccharides synthesis 80
YlPir1p Yarrowia lipolytica Yarrowia lipolytica lipase Lip2p Biochemical conversion 82
Eukaryotes / Multiple protein display
Pir1 / Pir2 S. cerevisiaeW303-1A, SSY18 α-1,2-galactosyltransferase from Schizosaccharomyces pombe; α-1,2-mannosyltransferase and a-1,3-mannosyltransferase from S. cerevisiae Oligosaccharide synthesis 78
α-Agglutinin (Aga1) S. cerevisiaeMT8-1 Expansin-like proteins (SWOI and AoelpI) from Trichoderma reesei and Aspergillus oryzae; Cellulases (EGII, CBHII and BGL) from T. reesei and Aspergillus aculeatus Ethanol production from cellulosic materials 92
Aga2p-fused scaffoldin (Minicellulosomes) S. cerevisiaeEBY100 Dockerin (docS and docA from Clostridium thermocellum)-fused EGII, CBHII and BGL Ethanol production from cellulosic materials 96
Aga2p-fused scaffoldin (Minicellulosomes) S. cerevisiaeEBY100, HZ848 Dockerin-fused EGII, CBHII, BGL, Thermoascus aurantiacus GH61a (lytic polysaccharide monooxygenases) and Humicola insolens cellobiose dehydrogenase Ethanol production from lignocellulose 97
Tab.1  Development of whole-cell biocatalysts by cell surface display systems
Fig.3  Development of the immobilized whole-cell catalyst by utilizing a cell surface adhesion. (A) A trimeric autotransporter adhesion, AtaA fiber, is involved in the adhesiveness and autoagglutination of Acinetobacter sp. Tol 5, and the fiber is encoded in single ataA gene; (B) gram-negative bacteria acquire adhesiveness and auto agglutinative property by heterologous expression of ataA gene. Those transformed bacteria can be immobilized to several abiotic materials
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