Microscale immobilized enzyme reactors in proteomics: Latest developments

Safdar M, Sproß J, Jaenis J (2014)
Journal of Chromatography A 1324: 1-10.

Journal Article | Published | English

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Abstract
Enzymatic digestion of proteins is one of the key steps in proteomic analyses. There has been a steady progress in the applied digestion protocols in the past, starting from conventional time-consuming in-solution or in-gel digestion protocols to rapid and efficient methods utilizing different types of microscale enzyme reactors. Application of such microreactors has been proven beneficial due to lower sample consumption, higher sensitivity and straightforward coupling with LC-MS set-ups. Novel stationary phases, immobilization techniques and device formats are being constantly developed and tested to optimize digestion efficiency of proteolytic enzymes. This review focuses on the latest developments associated with the preparation and application of microscale enzyme reactors for proteomics applications since 2008 onwards. A special attention has been paid to the discussion of different stationary phases applied for immobilization purposes. (C) 2013 Elsevier B.V. All rights reserved.
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Safdar M, Sproß J, Jaenis J. Microscale immobilized enzyme reactors in proteomics: Latest developments. Journal of Chromatography A. 2014;1324:1-10.
Safdar, M., Sproß, J., & Jaenis, J. (2014). Microscale immobilized enzyme reactors in proteomics: Latest developments. Journal of Chromatography A, 1324, 1-10.
Safdar, M., Sproß, J., and Jaenis, J. (2014). Microscale immobilized enzyme reactors in proteomics: Latest developments. Journal of Chromatography A 1324, 1-10.
Safdar, M., Sproß, J., & Jaenis, J., 2014. Microscale immobilized enzyme reactors in proteomics: Latest developments. Journal of Chromatography A, 1324, p 1-10.
M. Safdar, J. Sproß, and J. Jaenis, “Microscale immobilized enzyme reactors in proteomics: Latest developments”, Journal of Chromatography A, vol. 1324, 2014, pp. 1-10.
Safdar, M., Sproß, J., Jaenis, J.: Microscale immobilized enzyme reactors in proteomics: Latest developments. Journal of Chromatography A. 1324, 1-10 (2014).
Safdar, Muhammad, Sproß, Jens, and Jaenis, Janne. “Microscale immobilized enzyme reactors in proteomics: Latest developments”. Journal of Chromatography A 1324 (2014): 1-10.
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6 Citations in Europe PMC

Data provided by Europe PubMed Central.

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Wilson SR, Vehus T, Berg HS, Lundanes E., Bioanalysis 7(14), 2015
PMID: 26270786
Rational synthesis of novel recyclable Fe₃O₄@MOF nanocomposites for enzymatic digestion.
Zhao M, Zhang X, Deng C., Chem. Commun. (Camb.) 51(38), 2015
PMID: 25869528
Proteomics beyond trypsin.
Tsiatsiani L, Heck AJ., FEBS J. 282(14), 2015
PMID: 25823410
Open tubular lab-on-column/mass spectrometry for targeted proteomics of nanogram sample amounts.
Hustoft HK, Vehus T, Brandtzaeg OK, Krauss S, Greibrokk T, Wilson SR, Lundanes E., PLoS ONE 9(9), 2014
PMID: 25222838

118 References

Data provided by Europe PubMed Central.

Development of an automated digestion and droplet deposition microfluidic chip for MALDI-TOF MS.
Lee J, Musyimi HK, Soper SA, Murray KK., J. Am. Soc. Mass Spectrom. 19(7), 2008
PMID: 18479934
Rapid fabrication of glass/PDMS hybrid µIMER for high throughput membrane proteomics.
Pereira-Medrano AG, Forster S, Fowler GJ, McArthur SL, Wright PC., Lab Chip 10(24), 2010
PMID: 20949197
Proteolysis in microfluidic droplets: an approach to interface protein separation and peptide mass spectrometry.
Ji J, Nie L, Qiao L, Li Y, Guo L, Liu B, Yang P, Girault HH., Lab Chip 12(15), 2012
PMID: 22695710
Facile trypsin immobilization in polymeric membranes for rapid, efficient protein digestion.
Xu F, Wang WH, Tan YJ, Bruening ML., Anal. Chem. 82(24), 2010
PMID: 21087034
Prediction of protein orientation upon immobilization on biological and nonbiological surfaces.
Talasaz AH, Nemat-Gorgani M, Liu Y, Stahl P, Dutton RW, Ronaghi M, Davis RW., Proc. Natl. Acad. Sci. U.S.A. 103(40), 2006
PMID: 17001006
Rapid and enhanced proteolytic digestion using electric-field-oriented enzyme reactor.
Zhou Y, Yi T, Park SS, Chadwick W, Shen RF, Wu WW, Martin B, Maudsley S., J Proteomics 74(7), 2011
PMID: 21338726
Ion-exchange-membrane-based enzyme micro-reactor coupled online with liquid chromatography-mass spectrometry for protein analysis.
Zhou Z, Yang Y, Zhang J, Zhang Z, Bai Y, Liao Y, Liu H., Anal Bioanal Chem 403(1), 2012
PMID: 22349343

Starke, React. Funct. Polym. 73(), 2013

Jagur-Grodzinski, Polym. Adv. Technol. 21(), 2010

Oh, Can. J. Chem. 88(), 2010
Chitosan-based hydrogels for controlled, localized drug delivery.
Bhattarai N, Gunn J, Zhang M., Adv. Drug Deliv. Rev. 62(1), 2010
PMID: 19799949
Digital microfluidic hydrogel microreactors for proteomics.
Luk VN, Fiddes LK, Luk VM, Kumacheva E, Wheeler AR., Proteomics 12(9), 2012
PMID: 22589180
Trypsin-immobilized fiber core in syringe needle for highly efficient proteolysis.
Wang S, Chen Z, Yang P, Chen G., Proteomics 8(9), 2008
PMID: 18442168

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