메뉴 건너뛰기




Volumn 121, Issue 2, 2007, Pages 515-521

Immobilized tyrosinase reactor for on-line HPLC application. Development and characterization

Author keywords

HPLC; Immobilized enzyme; Kinetic parameters; Tyrosinase

Indexed keywords

ALDEHYDES; CATALYST ACTIVITY; CHEMICAL REACTORS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; POROUS MATERIALS; SUBSTRATES;

EID: 33846603694     PISSN: 09254005     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.snb.2006.04.076     Document Type: Article
Times cited : (23)

References (21)
  • 4
    • 0043051981 scopus 로고    scopus 로고
    • Oxidation of the flavonol quercetin by polyphenol oxidase
    • Jimenez M., and Garcia-Carmona F. Oxidation of the flavonol quercetin by polyphenol oxidase. J. Agric. Food Chem. 47 (1999) 56-60
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 56-60
    • Jimenez, M.1    Garcia-Carmona, F.2
  • 5
    • 0037010857 scopus 로고    scopus 로고
    • Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: a review
    • Duran N., Rosa M.A., D'Annibale A., and Gianfreda L. Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: a review. Enzyme Microb. Technol. 31 (2002) 907-931
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 907-931
    • Duran, N.1    Rosa, M.A.2    D'Annibale, A.3    Gianfreda, L.4
  • 6
    • 22844449351 scopus 로고    scopus 로고
    • Application of immobilized enzyme reactor in on-line high performance liquid chromatography: a review
    • Girelli A.M., and Mattei E. Application of immobilized enzyme reactor in on-line high performance liquid chromatography: a review. J. Chromatogr. B 819 (2005) 3-16
    • (2005) J. Chromatogr. B , vol.819 , pp. 3-16
    • Girelli, A.M.1    Mattei, E.2
  • 7
    • 0024328318 scopus 로고
    • Flow-injection determination of l-tyrosine in serum with an immobilized tyrosinase reactor and fluorescence detection
    • Kiba N., Ogi M., and Furusawa M. Flow-injection determination of l-tyrosine in serum with an immobilized tyrosinase reactor and fluorescence detection. Anal. Chim. Acta 224 (1989) 133-138
    • (1989) Anal. Chim. Acta , vol.224 , pp. 133-138
    • Kiba, N.1    Ogi, M.2    Furusawa, M.3
  • 8
    • 0027365771 scopus 로고
    • Post-column immobilized tyrosinase reactor for determination of l-3,4-dihydroxyphenylalanine and l-tyrosine by high-performance liquid chromatography with fluorescence detection
    • Kiba N., Itoi M., and Furusawa M. Post-column immobilized tyrosinase reactor for determination of l-3,4-dihydroxyphenylalanine and l-tyrosine by high-performance liquid chromatography with fluorescence detection. J. Chromatogr. 648 (1993) 481-484
    • (1993) J. Chromatogr. , vol.648 , pp. 481-484
    • Kiba, N.1    Itoi, M.2    Furusawa, M.3
  • 9
    • 1342308163 scopus 로고    scopus 로고
    • Monolithic micro-immobilized-enzyme reactor with human recombinant acetylcholinesterase for on-line inhibition studies
    • Bartolini M., Cavrini V., and Andrisano V. Monolithic micro-immobilized-enzyme reactor with human recombinant acetylcholinesterase for on-line inhibition studies. J. Chromatogr. A 1031 (2004) 27-34
    • (2004) J. Chromatogr. A , vol.1031 , pp. 27-34
    • Bartolini, M.1    Cavrini, V.2    Andrisano, V.3
  • 10
    • 0035848876 scopus 로고    scopus 로고
    • A chemically modified carbon paste electrode with-lactate dehydrogenase and alanine aminotranferase enzyme sequences for-lactic acid analysis
    • Shu H.C., and Wu N.P. A chemically modified carbon paste electrode with-lactate dehydrogenase and alanine aminotranferase enzyme sequences for-lactic acid analysis. Talanta 54 (2001) 361-368
    • (2001) Talanta , vol.54 , pp. 361-368
    • Shu, H.C.1    Wu, N.P.2
  • 11
    • 0347925059 scopus 로고    scopus 로고
    • Development and characterization of an immobilized enzyme reactor based on glyceraldehyde-3-phosphate dehydrogenase for on-line enzymatic studies
    • Bartolini M., Andrisano V., and Wainer I. Development and characterization of an immobilized enzyme reactor based on glyceraldehyde-3-phosphate dehydrogenase for on-line enzymatic studies. J. Chromatogr. A 987 (2003) 331-340
    • (2003) J. Chromatogr. A , vol.987 , pp. 331-340
    • Bartolini, M.1    Andrisano, V.2    Wainer, I.3
  • 12
    • 0017720495 scopus 로고
    • Comparison of intrinsic stabilities of free and bound enzymes by graphical removal of diffusional effects
    • Engasser J.M., and Coulet P.R. Comparison of intrinsic stabilities of free and bound enzymes by graphical removal of diffusional effects. Biochim. Biophys. Acta 485 (1977) 29-36
    • (1977) Biochim. Biophys. Acta , vol.485 , pp. 29-36
    • Engasser, J.M.1    Coulet, P.R.2
  • 13
    • 0032791826 scopus 로고    scopus 로고
    • Stereochemical resolution of racemates, in HPLC, using a chiral stationary phase based upon immobilized a-chymotrypsin. Part 1. Structural chiral separations
    • Felix G., and Descorps V. Stereochemical resolution of racemates, in HPLC, using a chiral stationary phase based upon immobilized a-chymotrypsin. Part 1. Structural chiral separations. Chromatographia 49 (1999) 595-605
    • (1999) Chromatographia , vol.49 , pp. 595-605
    • Felix, G.1    Descorps, V.2
  • 14
    • 0032793258 scopus 로고    scopus 로고
    • Stereochemical resolution of racemates, in HPLC, using a chiral stationary phase based upon immobilized a-chymotrypsin. Part 2. Enzyme chiral separations
    • Felix G., and Descorps V. Stereochemical resolution of racemates, in HPLC, using a chiral stationary phase based upon immobilized a-chymotrypsin. Part 2. Enzyme chiral separations. Chromatographia 49 (1999) 606-614
    • (1999) Chromatographia , vol.49 , pp. 606-614
    • Felix, G.1    Descorps, V.2
  • 15
    • 0001479670 scopus 로고
    • A simple ultraviolet spectrophotometric method for the determination of protein
    • Waddell W.J. A simple ultraviolet spectrophotometric method for the determination of protein. J. Lab. Clin. Med. 48 (1956) 311-314
    • (1956) J. Lab. Clin. Med. , vol.48 , pp. 311-314
    • Waddell, W.J.1
  • 16
    • 0021526156 scopus 로고
    • Tyrosine hydroxylase activity of immobilized tyrosinase on Enzacryl-AA and CPG-AA supports: stabilization and properties
    • Vilanova E., Manjon A., and Iborra J.L. Tyrosine hydroxylase activity of immobilized tyrosinase on Enzacryl-AA and CPG-AA supports: stabilization and properties. Biotechnol. Bioeng. 26 (1984) 1306-1312
    • (1984) Biotechnol. Bioeng. , vol.26 , pp. 1306-1312
    • Vilanova, E.1    Manjon, A.2    Iborra, J.L.3
  • 17
    • 2442555519 scopus 로고    scopus 로고
    • HPLC study of tyrosinase inhibition by thiopronine
    • Girelli A.M., Mattei E., and Messina A. HPLC study of tyrosinase inhibition by thiopronine. Biomed. Chromatogr. 18 (2004) 436-442
    • (2004) Biomed. Chromatogr. , vol.18 , pp. 436-442
    • Girelli, A.M.1    Mattei, E.2    Messina, A.3
  • 18
    • 0142074376 scopus 로고    scopus 로고
    • A novel method for the immobilization of tyrosinase to enhance stability
    • Sharma N.M., Kumar S., and Sawhney S.K. A novel method for the immobilization of tyrosinase to enhance stability. Biotechnol. Appl. Biochem. 38 (2003) 137-141
    • (2003) Biotechnol. Appl. Biochem. , vol.38 , pp. 137-141
    • Sharma, N.M.1    Kumar, S.2    Sawhney, S.K.3
  • 19
    • 0001064298 scopus 로고
    • Copper monooxygenases: tyrosinase and dopamine β-monooxygenase
    • Siegel H. (Ed), M. Dekker Inc., New York (Chapter 5)
    • Lerch K. Copper monooxygenases: tyrosinase and dopamine β-monooxygenase. In: Siegel H. (Ed). Metal Ions in Biological Systems vol. 13 (1981), M. Dekker Inc., New York 143-186 (Chapter 5)
    • (1981) Metal Ions in Biological Systems , vol.13 , pp. 143-186
    • Lerch, K.1
  • 20
    • 0001012399 scopus 로고
    • Polyphenoloxidase from apple, partial purification and some properties
    • Janovitz-Klapp A., Richard F., and Nicholas J. Polyphenoloxidase from apple, partial purification and some properties. Phytochemistry 28 (1989) 2903-2907
    • (1989) Phytochemistry , vol.28 , pp. 2903-2907
    • Janovitz-Klapp, A.1    Richard, F.2    Nicholas, J.3
  • 21
    • 0000832894 scopus 로고
    • Wingard L.B., Katchalski Kazir E., and Goldstein L. (Eds), Academic Press, New York
    • Engasser J.-M., and Horvath H. In: Wingard L.B., Katchalski Kazir E., and Goldstein L. (Eds). Applied Biochemistry and Bioengineering vol. 1 (1976), Academic Press, New York 127-220
    • (1976) Applied Biochemistry and Bioengineering , vol.1 , pp. 127-220
    • Engasser, J.-M.1    Horvath, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.