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Volumn 1440, Issue , 2016, Pages 45-54

Preparation and evaluation of dual-enzyme microreactor with co-immobilized trypsin and chymotrypsin

Author keywords

Capillary liquid chromatography; Chymotrypsin; Immobilized enzyme microreactor; Proteomics; Transferrin; Trypsin

Indexed keywords

ACRYLIC MONOMERS; AMINO ACIDS; CHEMICAL REACTORS; COSTS; EFFICIENCY; ENZYME IMMOBILIZATION; ETHYLENE; ETHYLENE GLYCOL; FUSED SILICA; GAS METAL ARC WELDING; PETROLEUM RESERVOIR EVALUATION; PROTEOMICS;

EID: 84977861268     PISSN: 00219673     EISSN: 18733778     Source Type: Journal    
DOI: 10.1016/j.chroma.2016.02.070     Document Type: Article
Times cited : (42)

References (43)
  • 2
    • 0033818431 scopus 로고    scopus 로고
    • Biomedical application of immobilized enzymes
    • Liang J.F., Li Y.T., Yang V.C. Biomedical application of immobilized enzymes. J. Pharm. Sci. 2000, 89:979-990.
    • (2000) J. Pharm. Sci. , vol.89 , pp. 979-990
    • Liang, J.F.1    Li, Y.T.2    Yang, V.C.3
  • 3
    • 33645466806 scopus 로고    scopus 로고
    • Less common applications of monoliths: I. Microscale protein mapping with proteolytic enzymes immobilized on monolithic supports
    • Svec F. Less common applications of monoliths: I. Microscale protein mapping with proteolytic enzymes immobilized on monolithic supports. Electrophoresis 2006, 27:947-961.
    • (2006) Electrophoresis , vol.27 , pp. 947-961
    • Svec, F.1
  • 4
    • 65449162340 scopus 로고    scopus 로고
    • Less common applications of monoliths: IV. Recent developments in immobilized enzyme reactors for proteomics and biotechnology
    • Krenkova J., Svec F. Less common applications of monoliths: IV. Recent developments in immobilized enzyme reactors for proteomics and biotechnology. J. Sep. Sci. 2009, 32:706-718.
    • (2009) J. Sep. Sci. , vol.32 , pp. 706-718
    • Krenkova, J.1    Svec, F.2
  • 5
    • 84155170822 scopus 로고    scopus 로고
    • Fabrication of tunable microreactor with enzyme modified magnetic nanoparticles for microfluidic electrochemical detection of glucose
    • Sheng J., Zhang L., Lei J., Ju Hu. Fabrication of tunable microreactor with enzyme modified magnetic nanoparticles for microfluidic electrochemical detection of glucose. Anal. Chim. Acta 2012, 709:41-46.
    • (2012) Anal. Chim. Acta , vol.709 , pp. 41-46
    • Sheng, J.1    Zhang, L.2    Lei, J.3    Ju, H.4
  • 6
    • 84872301911 scopus 로고    scopus 로고
    • Lipase Immobilized methacrylate polymer monolith microreactor for lipid transformations and online analytics
    • Mugo S.M., Ayton K. Lipase Immobilized methacrylate polymer monolith microreactor for lipid transformations and online analytics. J. Am. Oil Chem. Soc. 2013, 90:65-72.
    • (2013) J. Am. Oil Chem. Soc. , vol.90 , pp. 65-72
    • Mugo, S.M.1    Ayton, K.2
  • 7
    • 84870901778 scopus 로고    scopus 로고
    • On-line immobilized acetylcholinesterase microreactor for screening of inhibitors from natural extracts by capillary electrophoresis
    • Min W., Wang W., Chen J., Wang A., Hu Z. On-line immobilized acetylcholinesterase microreactor for screening of inhibitors from natural extracts by capillary electrophoresis. Anal. Bioanal. Chem. 2012, 404:2397-2405.
    • (2012) Anal. Bioanal. Chem. , vol.404 , pp. 2397-2405
    • Min, W.1    Wang, W.2    Chen, J.3    Wang, A.4    Hu, Z.5
  • 8
    • 84872598761 scopus 로고    scopus 로고
    • Microchip CE-LIF method for the hydrolysis of l-glutamine by using L-asparaginase enzyme reactor based on gold nanoparticle
    • Qiao J., Qi L., Yan H., Li Y., Mu X. Microchip CE-LIF method for the hydrolysis of l-glutamine by using L-asparaginase enzyme reactor based on gold nanoparticle. Electrophoresis 2013, 34:409-416.
    • (2013) Electrophoresis , vol.34 , pp. 409-416
    • Qiao, J.1    Qi, L.2    Yan, H.3    Li, Y.4    Mu, X.5
  • 10
    • 42349103426 scopus 로고    scopus 로고
    • Organic-inorganic hybrid silica monolith based immobilized trypsin reactor with high enzymatic activity
    • Ma J., Liang Z., Qiao X., Deng Q., Tao D., Zhang L., Zhang Y. Organic-inorganic hybrid silica monolith based immobilized trypsin reactor with high enzymatic activity. Anal. Chem. 2008, 80:2949-2956.
    • (2008) Anal. Chem. , vol.80 , pp. 2949-2956
    • Ma, J.1    Liang, Z.2    Qiao, X.3    Deng, Q.4    Tao, D.5    Zhang, L.6    Zhang, Y.7
  • 12
    • 64749088652 scopus 로고    scopus 로고
    • Highly efficient enzyme reactors containing trypsin and endoproteinase LysC immobilized on porous polymer monolith coupled to MS suitable for analysis of antibodies
    • Krenkova J., Lacher N.A., Svec F. Highly efficient enzyme reactors containing trypsin and endoproteinase LysC immobilized on porous polymer monolith coupled to MS suitable for analysis of antibodies. Anal. Chem. 2009, 81:2004-2012.
    • (2009) Anal. Chem. , vol.81 , pp. 2004-2012
    • Krenkova, J.1    Lacher, N.A.2    Svec, F.3
  • 13
    • 3042579869 scopus 로고    scopus 로고
    • On-line protein digestion and peptide mapping by capillary electrophoresis with post-column labeling for laser-induced fluorescence detection
    • Ye M.L., Hu S., Schoenherr R.M., Dovichi N.J. On-line protein digestion and peptide mapping by capillary electrophoresis with post-column labeling for laser-induced fluorescence detection. Electrophoresis 2004, 25:1319-1326.
    • (2004) Electrophoresis , vol.25 , pp. 1319-1326
    • Ye, M.L.1    Hu, S.2    Schoenherr, R.M.3    Dovichi, N.J.4
  • 14
    • 78751584674 scopus 로고    scopus 로고
    • High throughput tryptic digestion via poly(acrylamide-co-methylenebisacrylamide) monolith based immobilized enzyme reactor
    • Wu S., Sun L., Ma J., Yang K., Liang Z., Zhang L., Zhang Y. High throughput tryptic digestion via poly(acrylamide-co-methylenebisacrylamide) monolith based immobilized enzyme reactor. Talanta 2011, 83:1748-1753.
    • (2011) Talanta , vol.83 , pp. 1748-1753
    • Wu, S.1    Sun, L.2    Ma, J.3    Yang, K.4    Liang, Z.5    Zhang, L.6    Zhang, Y.7
  • 15
    • 79955080967 scopus 로고    scopus 로고
    • Hydrophilic monolith based immobilized enzyme reactors in capillary and on microchip for high-throughput proteomic analysis
    • Liang Y., Tao D., Ma J., Sun L., Liang Z., Zhang L., Zhang Y. Hydrophilic monolith based immobilized enzyme reactors in capillary and on microchip for high-throughput proteomic analysis. J. Chromatogr. A 2011, 1218:2898-2905.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 2898-2905
    • Liang, Y.1    Tao, D.2    Ma, J.3    Sun, L.4    Liang, Z.5    Zhang, L.6    Zhang, Y.7
  • 16
    • 32144464053 scopus 로고    scopus 로고
    • Rapid protein identification using monolithic enzymatic microreactor and LC-ESI-MS/MS
    • Duan J., Liang Z., Yang C., Zhang J., Zhang L., Zhang W., Zhan Y. Rapid protein identification using monolithic enzymatic microreactor and LC-ESI-MS/MS. Proteomics 2006, 6:412-419.
    • (2006) Proteomics , vol.6 , pp. 412-419
    • Duan, J.1    Liang, Z.2    Yang, C.3    Zhang, J.4    Zhang, L.5    Zhang, W.6    Zhan, Y.7
  • 17
    • 36949024716 scopus 로고    scopus 로고
    • Chymotrypsin immobilization on epoxy monolithic silica columns: development and characterization of a bioreactor for protein digestion
    • Temporini C., Calleri E., Campese D., Cabrera K., Felix G., Massolini G. Chymotrypsin immobilization on epoxy monolithic silica columns: development and characterization of a bioreactor for protein digestion. J. Sep. Sci. 2007, 30:3069-3076.
    • (2007) J. Sep. Sci. , vol.30 , pp. 3069-3076
    • Temporini, C.1    Calleri, E.2    Campese, D.3    Cabrera, K.4    Felix, G.5    Massolini, G.6
  • 18
    • 84863781029 scopus 로고    scopus 로고
    • Synthesis of a monolithic, micro-immobilised enzyme reactor via click-chemistry
    • Çelebi B., Bayraktar A., Tuncel A. Synthesis of a monolithic, micro-immobilised enzyme reactor via click-chemistry. Anal. Bioanal. Chem. 2012, 403:2655-2663.
    • (2012) Anal. Bioanal. Chem. , vol.403 , pp. 2655-2663
    • Çelebi, B.1    Bayraktar, A.2    Tuncel, A.3
  • 19
    • 0037026429 scopus 로고    scopus 로고
    • High-performance affinity chromatography for characterization of human immunoglobulin G digestion with papain
    • Luo Q., Mao X., Kong L., Huang X., Zou H. High-performance affinity chromatography for characterization of human immunoglobulin G digestion with papain. J. Chromatogr. B 2002, 776:139-147.
    • (2002) J. Chromatogr. B , vol.776 , pp. 139-147
    • Luo, Q.1    Mao, X.2    Kong, L.3    Huang, X.4    Zou, H.5
  • 20
    • 84864415350 scopus 로고    scopus 로고
    • A novel approach for efficient immobilization and stabilization of papain on magnetic gold nanocomposites
    • Sahoo B., Sahu S.K., Bhattacharya D., Dhara D., Pramanik P. A novel approach for efficient immobilization and stabilization of papain on magnetic gold nanocomposites. Colloids Surf. B: Biointerfaces 2013, 101:280-289.
    • (2013) Colloids Surf. B: Biointerfaces , vol.101 , pp. 280-289
    • Sahoo, B.1    Sahu, S.K.2    Bhattacharya, D.3    Dhara, D.4    Pramanik, P.5
  • 21
    • 80053121939 scopus 로고    scopus 로고
    • Immobilization and stabilization of papain on poly(hydroxyethyl methacrylate-ethylenglycol dimethacrylate) beads grafted with epoxy functional polymer chains via surface-initiated-atom transfer radical polymerization (SI-ATRP)
    • Bayramoglu G., Senkal B.F., Yilmaz M., Arica M.Y. Immobilization and stabilization of papain on poly(hydroxyethyl methacrylate-ethylenglycol dimethacrylate) beads grafted with epoxy functional polymer chains via surface-initiated-atom transfer radical polymerization (SI-ATRP). Bioresour. Technol. 2011, 102:9833-9837.
    • (2011) Bioresour. Technol. , vol.102 , pp. 9833-9837
    • Bayramoglu, G.1    Senkal, B.F.2    Yilmaz, M.3    Arica, M.Y.4
  • 22
    • 41549110915 scopus 로고    scopus 로고
    • In-line system containing porous polymer monoliths for protein digestion with immobilized pepsin, peptide preconcentration and nano-liquid chromatography separation coupled to electrospray ionization mass spectroscopy
    • Geiser L., Eeltink S., Svec F., Frechet J.M.J. In-line system containing porous polymer monoliths for protein digestion with immobilized pepsin, peptide preconcentration and nano-liquid chromatography separation coupled to electrospray ionization mass spectroscopy. J. Chromatogr. A 2008, 1188:88-96.
    • (2008) J. Chromatogr. A , vol.1188 , pp. 88-96
    • Geiser, L.1    Eeltink, S.2    Svec, F.3    Frechet, J.M.J.4
  • 25
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick D.S., Gerber S.A., Gygi S.P. The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 2005, 35:265-273.
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 27
    • 84879143783 scopus 로고    scopus 로고
    • Development of glutaraldehyde-crosslinked chymotrypsin and an in situ immobilized enzyme microreactor with peptide mapping by capillary electrophoresis
    • Ghafourifar G., Fleitz A., Waldron K.C. Development of glutaraldehyde-crosslinked chymotrypsin and an in situ immobilized enzyme microreactor with peptide mapping by capillary electrophoresis. Electrophoresis 2013, 34:1804-1811.
    • (2013) Electrophoresis , vol.34 , pp. 1804-1811
    • Ghafourifar, G.1    Fleitz, A.2    Waldron, K.C.3
  • 28
    • 77956877523 scopus 로고    scopus 로고
    • Multidigestion in continuous flow tandem protease-immobilized microreactors for proteomic analysis
    • Yamaguchi H., Miyazaki M., Kawazumi H., Maeda H. Multidigestion in continuous flow tandem protease-immobilized microreactors for proteomic analysis. Anal. Biochem. 2010, 407:12-18.
    • (2010) Anal. Biochem. , vol.407 , pp. 12-18
    • Yamaguchi, H.1    Miyazaki, M.2    Kawazumi, H.3    Maeda, H.4
  • 29
    • 84924339515 scopus 로고    scopus 로고
    • Investigation of bi-enzymatic reactor based on hybrid monolith with nanoparticles embedded and its proteolytic characteristics
    • Shangguana L., Zhang L., Xiong Z., Ren J., Zhang R., Gao F., Zhang W. Investigation of bi-enzymatic reactor based on hybrid monolith with nanoparticles embedded and its proteolytic characteristics. J. Chromatogr. A 2015, 1388:158-166.
    • (2015) J. Chromatogr. A , vol.1388 , pp. 158-166
    • Shangguana, L.1    Zhang, L.2    Xiong, Z.3    Ren, J.4    Zhang, R.5    Gao, F.6    Zhang, W.7
  • 30
    • 0030634860 scopus 로고    scopus 로고
    • Modified PMMA monosize microbeads for glucose oxidase immobilization
    • Bulmq V., Ayhan H., Pigkin E. Modified PMMA monosize microbeads for glucose oxidase immobilization. Chem. Eng. J. 1997, 65:71-76.
    • (1997) Chem. Eng. J. , vol.65 , pp. 71-76
    • Bulmq, V.1    Ayhan, H.2    Pigkin, E.3
  • 31
    • 0035813506 scopus 로고    scopus 로고
    • Immobilization of trypsin on polyester fleece via different spacers
    • Nouaimi M., Moschel K., Bisswanger H. Immobilization of trypsin on polyester fleece via different spacers. Enzyme Microb. Technol. 2001, 29:567-574.
    • (2001) Enzyme Microb. Technol. , vol.29 , pp. 567-574
    • Nouaimi, M.1    Moschel, K.2    Bisswanger, H.3
  • 32
    • 0034672424 scopus 로고    scopus 로고
    • On-line characterization of the activity and reaction kinetics of immobilized enzyme by high-performance frontal analysis
    • Jiang H., Zou H., Wang H., Ni J., Zhang Q., Zhang Y. On-line characterization of the activity and reaction kinetics of immobilized enzyme by high-performance frontal analysis. J. Chromatogr. A 2000, 903:77-84.
    • (2000) J. Chromatogr. A , vol.903 , pp. 77-84
    • Jiang, H.1    Zou, H.2    Wang, H.3    Ni, J.4    Zhang, Q.5    Zhang, Y.6
  • 33
    • 34948845083 scopus 로고    scopus 로고
    • Immobilization of trypsin on superparamagnetic nanoparticles for rapid and effective proteolysis
    • Li Y., Xu X., Deng C., Yang P., Zhang X. Immobilization of trypsin on superparamagnetic nanoparticles for rapid and effective proteolysis. J. Proteome Res. 2007, 6:3849-3855.
    • (2007) J. Proteome Res. , vol.6 , pp. 3849-3855
    • Li, Y.1    Xu, X.2    Deng, C.3    Yang, P.4    Zhang, X.5
  • 34
    • 67649678443 scopus 로고    scopus 로고
    • On-line multi-enzymatic approach for improved sequence coverage in protein analysis
    • Temporini C., Calleri E., Cabrera K., Felix G., Massolini G. On-line multi-enzymatic approach for improved sequence coverage in protein analysis. J. Sep. Sci. 2009, 32:1120-1128.
    • (2009) J. Sep. Sci. , vol.32 , pp. 1120-1128
    • Temporini, C.1    Calleri, E.2    Cabrera, K.3    Felix, G.4    Massolini, G.5
  • 35
    • 0038070646 scopus 로고    scopus 로고
    • On-column digestion of proteins in aqueous-organic solvents
    • Slysz G.W., Schriemer D.C. On-column digestion of proteins in aqueous-organic solvents. Rapid Commun. Mass Spectrom. 2003, 17:1044-1050.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1044-1050
    • Slysz, G.W.1    Schriemer, D.C.2
  • 36
    • 84872832876 scopus 로고    scopus 로고
    • Disparities between immobilized enzyme and solution based digestion of transferrin with trypsin
    • Rivera-Burgos D., Regnier F.E. Disparities between immobilized enzyme and solution based digestion of transferrin with trypsin. J. Sep. Sci. 2013, 36:454-460.
    • (2013) J. Sep. Sci. , vol.36 , pp. 454-460
    • Rivera-Burgos, D.1    Regnier, F.E.2
  • 37
    • 84903650406 scopus 로고    scopus 로고
    • HPLC separation of casein components on a diol-bonded silica column with MALDI TOF/TOF MS identification
    • Pomastowski P., Walczak J., Gawin M., Bocian S., Piekoszewski W., Buszewski B. HPLC separation of casein components on a diol-bonded silica column with MALDI TOF/TOF MS identification. Anal. Methods 2014, 6:5236-5244.
    • (2014) Anal. Methods , vol.6 , pp. 5236-5244
    • Pomastowski, P.1    Walczak, J.2    Gawin, M.3    Bocian, S.4    Piekoszewski, W.5    Buszewski, B.6
  • 38
    • 0033524379 scopus 로고    scopus 로고
    • Design of reactive porous polymer supports for high throughput bioreactors: poly(2-vinyl-4,4-dimethylazlactone-co-acrylamide-co-ethylene dimethacrylate) monoliths
    • Xie S., Svec F., Fréchet J.M.J. Design of reactive porous polymer supports for high throughput bioreactors: poly(2-vinyl-4,4-dimethylazlactone-co-acrylamide-co-ethylene dimethacrylate) monoliths. Biotechnol. Bioeng. 1999, 62:30-35.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 30-35
    • Xie, S.1    Svec, F.2    Fréchet, J.M.J.3
  • 39
    • 70349759691 scopus 로고    scopus 로고
    • Novel monolithic enzymatic microreactor based on single-enzyme nanoparticles for highly efficient proteolysis and its application in multidimensional liquid chromatography
    • Gao M., Zhang P., Hong G., Guan X., Yan G., Deng C., Zhang X. Novel monolithic enzymatic microreactor based on single-enzyme nanoparticles for highly efficient proteolysis and its application in multidimensional liquid chromatography. J. Chromatogr. A 2009, 1216:7472-7477.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 7472-7477
    • Gao, M.1    Zhang, P.2    Hong, G.3    Guan, X.4    Yan, G.5    Deng, C.6    Zhang, X.7
  • 40
    • 79954632927 scopus 로고    scopus 로고
    • Immobilization of trypsin on sub-micron skeletal polymer monolith
    • Yao C., Qi L., Hu W., Wang F., Yang G. Immobilization of trypsin on sub-micron skeletal polymer monolith. Anal. Chim. Acta 2011, 692:131-137.
    • (2011) Anal. Chim. Acta , vol.692 , pp. 131-137
    • Yao, C.1    Qi, L.2    Hu, W.3    Wang, F.4    Yang, G.5
  • 41
    • 82955163251 scopus 로고    scopus 로고
    • Immobilized trypsin on epoxy organic monoliths with modulated hydrophilicity: novel bioreactors useful for protein analysis by liquid chromatography coupled to tandem mass spectrometry
    • Calleri E., Temporini C., Gasparrini F., Simone P., Villani C., Ciogli A., Massolini G. Immobilized trypsin on epoxy organic monoliths with modulated hydrophilicity: novel bioreactors useful for protein analysis by liquid chromatography coupled to tandem mass spectrometry. J. Chromatogr. A 2011, 1218:8937-8945.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 8937-8945
    • Calleri, E.1    Temporini, C.2    Gasparrini, F.3    Simone, P.4    Villani, C.5    Ciogli, A.6    Massolini, G.7
  • 42
    • 84881190519 scopus 로고    scopus 로고
    • Activity of the integrated on-line trypsin microreactor and nanoelectrospray emitter in acetonitrile-water co-solvent mixtures
    • Long Y., Wood T.D. Activity of the integrated on-line trypsin microreactor and nanoelectrospray emitter in acetonitrile-water co-solvent mixtures. Microfluid. Nanofluid. 2013, 15:57-64.
    • (2013) Microfluid. Nanofluid. , vol.15 , pp. 57-64
    • Long, Y.1    Wood, T.D.2
  • 43
    • 84881347961 scopus 로고    scopus 로고
    • Preparation of a dual-enzyme co-immobilized capillary microreactor and simultaneous screening of multiple enzyme inhibitors by capillary electrophoresis
    • Lin P., Zhao S., Lu X., Ye F., Wang H. Preparation of a dual-enzyme co-immobilized capillary microreactor and simultaneous screening of multiple enzyme inhibitors by capillary electrophoresis. J. Sep. Sci. 2013, 36:2538-2543.
    • (2013) J. Sep. Sci. , vol.36 , pp. 2538-2543
    • Lin, P.1    Zhao, S.2    Lu, X.3    Ye, F.4    Wang, H.5


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