Improvement of downstream processing of recombinant proteins by means of genetic engineering

Flaschel E, Friehs K (1993)
Biotechnology Advances 11(1): 31-77.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
Abstract / Bemerkung
The rapid advancement of genetic engineering has allowed to produce an impressive number of proteins on a scale which would not have been achieved by classical biotechnology. At the beginning of this development research was focussed on elucidating the mechanisms of protein overexpression. The appearance of inclusion bodies may illustrate the success. In the meantime, genetic engineering is not only expected to achieve overexpression, but to improve the whole process of protein production. For downstream processing of recombinant proteins, the synthesis of fusion proteins is of primary importance. Fusion with certain proteins or peptides may protect the target protein from proteolytic degradation and may alter its solubility. Intracellular proteins may be translocated by means of fusions with signal peptides. Affinity tags as fusion complements may render protein separation and purification highly selective. These methods as well as similar ones for improving the downstream processing of proteins will be discussed on the basis of recent literature.
Biotechnology Advances
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Flaschel E, Friehs K. Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances. 1993;11(1):31-77.
Flaschel, E., & Friehs, K. (1993). Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances, 11(1), 31-77.
Flaschel, Erwin, and Friehs, Karl. 1993. “Improvement of downstream processing of recombinant proteins by means of genetic engineering”. Biotechnology Advances 11 (1): 31-77.
Flaschel, E., and Friehs, K. (1993). Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances 11, 31-77.
Flaschel, E., & Friehs, K., 1993. Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances, 11(1), p 31-77.
E. Flaschel and K. Friehs, “Improvement of downstream processing of recombinant proteins by means of genetic engineering”, Biotechnology Advances, vol. 11, 1993, pp. 31-77.
Flaschel, E., Friehs, K.: Improvement of downstream processing of recombinant proteins by means of genetic engineering. Biotechnology Advances. 11, 31-77 (1993).
Flaschel, Erwin, and Friehs, Karl. “Improvement of downstream processing of recombinant proteins by means of genetic engineering”. Biotechnology Advances 11.1 (1993): 31-77.
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Ellis J., Nature 358(6383), 1992
PMID: 1352857
TCP1 complex is a molecular chaperone in tubulin biogenesis.
Yaffe MB, Farr GW, Miklos D, Horwich AL, Sternlicht ML, Sternlicht H., Nature 358(6383), 1992
PMID: 1630491
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol.
Lewis VA, Hynes GM, Zheng D, Saibil H, Willison K., Nature 358(6383), 1992
PMID: 1630492
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.
Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU., Nature 356(6371), 1992
PMID: 1349157
Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase.
Buchner J, Brinkmann U, Pastan I., Biotechnology (N.Y.) 10(6), 1992
PMID: 1369490
Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding
Schönbrunner, 1992
An evaluation of different enzymatic cleavage methods for recombinant fusion proteins, applied on des(1-3)insulin-like growth factor I.
Forsberg G, Baastrup B, Rondahl H, Holmgren E, Pohl G, Hartmanis M, Lake M., J. Protein Chem. 11(2), 1992
PMID: 1388667
Production of recombinant human glucagon in the form of a fusion protein in Escherichia coli; recovery of glucagon by sequence-specific digestion.
Ishizaki J, Tamaki M, Shin M, Tsuzuki H, Yoshikawa K, Teraoka H, Yoshida N., Appl. Microbiol. Biotechnol. 36(4), 1992
PMID: 1368201
Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex.
Luirink J, High S, Wood H, Giner A, Tollervey D, Dobberstein B., Nature 359(6397), 1992
PMID: 1279430
The E. coli ffh gene is necessary for viability and efficient protein export.
Phillips GJ, Silhavy TJ., Nature 359(6397), 1992
PMID: 1331806
Transfer and Expression of Heterologous Genes in Yeasts Other Than Saccharomyces cerevisiae
Reiser, Adv. Biochem. Eng./Biotechnol. 43(), 1990
Die methylotrophe Hefe Hansenula polymorpha als Expressionssystem für heterologe Proteine
Gellissen, BioEng. 5(), 1990
Kluyveromyces as a host for heterologous gene expression: expression and secretion of prochymosin.
van den Berg JA, van der Laken KJ, van Ooyen AJ, Renniers TC, Rietveld K, Schaap A, Brake AJ, Bishop RJ, Schultz K, Moyer D., Biotechnology (N.Y.) 8(2), 1990
PMID: 1366557
Genetics and Genetic Engineering of the Industrial Yeast Yarrowia lipolytica
Heslot, Adv. Biochem. Eng./Biotechnol. 43(), 1990
Transformation of different strains of Escherichia coli with multicopy plasmids carrying the phoA gene causes the secretion of periplasmic alkaline phosphatase and the accumulation of its precursor
Nesmeyanova, Mol. Biol. 25(3), 1991
Rites of passage: moving biotech proteins through the ER.
Edgington SM., Biotechnology (N.Y.) 10(11), 1992
PMID: 1369017

Production of Recombinant Porcine Tumor Necrosis Factor Alpha in a Novel E. coli Expression System
Su, Bio/Technol. 13(5), 1992
A Modified Vector for the Controlled High-Level Overproduction of Staphylococcal Protein A Fusion Proteins in the Periplasm of Escherichia coli
Engel, Protein Expression Purification 3(), 1992
Fusions to the 5' end of a gene encoding a two-domain analogue of staphylococcal protein A.
Rondahl H, Nilsson B, Holmgren E., J. Biotechnol. 25(3), 1992
PMID: 1368804

Single-step purification on DEAE-sephacel of recombinant polypeptides produced in Escherichia coli.
Ortega S, Garcia JL, Zazo M, Varela J, Munoz-Willery I, Cuevas P, Gimenez-Gallego G., Biotechnology (N.Y.) 10(7), 1992
PMID: 1377476
Immobilization and single-step purification of fusion proteins using DEAE-cellulose.
Sanchez-Puelles JM, Sanz JM, Garcia JL, Garcia E., Eur. J. Biochem. 203(1-2), 1992
PMID: 1730220
A universal expression-purification system based on the coiled-coil interaction of myosin heavy chain.
Wolber V, Maeda K, Schumann R, Brandmeier B, Wiesmuller L, Wittinghofer A., Biotechnology (N.Y.) 10(8), 1992
PMID: 1368985

Molecular and cellular targeting in the expression of foreign polypeptides in bacteria.
Clement JM, Charbit A, Leclerc C, Martineau P, Muir S, O'Callaghan D, Popescu O, Szmelcman S, Hofnung M., Antonie Van Leeuwenhoek 61(2), 1992
PMID: 1580616
Protein secretion in gram-positive bacteria.
Freudl R., J. Biotechnol. 23(3), 1992
PMID: 1368245
Enhanced production and recovery of recombinant proteins genetically targeted into the periplasm - E. coli penicillin acylase as an initial model system
Glisin, 1991
Human hemoglobin expression in Escherichia coli: importance of optimal codon usage.
Hernan RA, Hui HL, Andracki ME, Noble RW, Sligar SG, Walder JA, Walder RY., Biochemistry 31(36), 1992
PMID: 1390646
Protein folding and its implications for the production of recombinant proteins.
Hlodan R, Craig S, Pain RH., Biotechnol. Genet. Eng. Rev. 9(), 1991
PMID: 1797019


Keil, 1992
Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation.
Kiefhaber T, Rudolph R, Kohler HH, Buchner J., Biotechnology (N.Y.) 9(9), 1991
PMID: 1367356
Proteolytic response to the expression of an abnormal beta-galactosidase in Escherichia coli.
Kosinski MJ, Rinas U, Bailey JE., Appl. Microbiol. Biotechnol. 37(3), 1992
PMID: 1368906
Stabilization of recombinant proteins from proteolytic degradation in Escherichia coli using a dual affinity fusion strategy.
Murby M, Cedergren L, Nilsson J, Nygren PA, Hammarberg B, Nilsson B, Enfors SO, Uhlen M., Biotechnol. Appl. Biochem. 14(3), 1991
PMID: 1777118
Secretion incompetence of bovine pancreatic trypsin inhibitor expressed in Escherichia coli.
Nilsson B, Berman-Marks C, Kuntz ID, Anderson S., J. Biol. Chem. 266(5), 1991
PMID: 1704370
Cell-free translation systems may provide new bioprocessing techniques
Orr, Gen. Eng. News (), 1989
Cell-free translation systems may provide new bioprocessing techniques
Orr, Gen. Eng. News (), 1989
Sequence-specific cleavage of protein fusions using a recombinant Neisseria type 2 IgA protease.
Pohlner J, Klauser T, Kuttler E, Halter R., Biotechnology (N.Y.) 10(7), 1992
PMID: 1368270
High-level temperature-induced synthesis of an antibody VH-domain in Escherichia coli using the PelB secretion signal.
Power BE, Ivancic N, Harley VR, Webster RG, Kortt AA, Irving RA, Hudson PJ., Gene 113(1), 1992
PMID: 1563636
Cysteine to serine substitutions in basic fibroblast growth factor: effect on inclusion body formation and proteolytic susceptibility during in vitro refolding.
Rinas U, Tsai LB, Lyons D, Fox GM, Stearns G, Fieschko J, Fenton D, Bailey JE., Biotechnology (N.Y.) 10(4), 1992
PMID: 1368488
In-vitro cleavage of a fusion protein bound to cellulose using the soluble yscFs (Kex2) variant.
Seeboth PG, Warren RA, Heim J., Appl. Microbiol. Biotechnol. 37(5), 1992
PMID: 1368916
A pH regulated promoter for the expression of recombinant proteins in Escherichia coli
Tolentino, Biotechnol. Lett. 14(), 1992

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