메뉴 건너뛰기




Volumn 152, Issue 1-2, 2011, Pages 30-36

Activity and stability of cross-linked tyrosinase aggregates in aqueous and nonaqueous media

Author keywords

Cross linked enzyme aggregates (CLEAs); Ionic liquids (ILs); Organic solvents; Thermodynamic water activity; Tyrosinase

Indexed keywords

, INHIBITOR; AMMONIUM SULFATE; AQUEOUS SOLUTIONS; CROSS-LINKED ENZYME AGGREGATES; GLUTARALDEHYDES; NONAQUEOUS MEDIA; ORGANIC MEDIA; TERT BUTANOL; TYROSINASE; WATER ACTIVITY;

EID: 79952036654     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.01.014     Document Type: Article
Times cited : (73)

References (34)
  • 1
    • 0002461353 scopus 로고    scopus 로고
    • Modes of using enzymes in organic media
    • Blackie Academic & Professional, New York, A.M.P. Koskinen, A.M. Klibanov (Eds.)
    • Adlercreutz P. Modes of using enzymes in organic media. Enzymatic Reactions in Organic Media 1996, 9-42. Blackie Academic & Professional, New York. A.M.P. Koskinen, A.M. Klibanov (Eds.).
    • (1996) Enzymatic Reactions in Organic Media , pp. 9-42
    • Adlercreutz, P.1
  • 2
    • 38049085641 scopus 로고    scopus 로고
    • Preparation of cross-linked tyrosinase aggregates
    • Aytar B.S., Bakir U. Preparation of cross-linked tyrosinase aggregates. Process Biochem. 2008, 43:125-131.
    • (2008) Process Biochem. , vol.43 , pp. 125-131
    • Aytar, B.S.1    Bakir, U.2
  • 3
    • 34848883383 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals
    • Cabana H., Jones J.P., Agathos S.N. Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals. J. Biotechnol. 2007, 132:23-31.
    • (2007) J. Biotechnol. , vol.132 , pp. 23-31
    • Cabana, H.1    Jones, J.P.2    Agathos, S.N.3
  • 4
    • 0035931490 scopus 로고    scopus 로고
    • Cross-linked aggregates of penicillin acylase: robust catalysts for the synthesis of β-lactam antibiotics
    • Cao L., van Langen L.M., van Rantwijk F., Sheldon R.A. Cross-linked aggregates of penicillin acylase: robust catalysts for the synthesis of β-lactam antibiotics. J. Mol. Catal. B: Enzym. 2001, 11:665-670.
    • (2001) J. Mol. Catal. B: Enzym. , vol.11 , pp. 665-670
    • Cao, L.1    van Langen, L.M.2    van Rantwijk, F.3    Sheldon, R.A.4
  • 5
    • 33846489558 scopus 로고    scopus 로고
    • Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions
    • Dalal S., Kapoor M., Gupta M.N. Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions. J. Mol. Catal. B: Enzym. 2007, 44:128-132.
    • (2007) J. Mol. Catal. B: Enzym. , vol.44 , pp. 128-132
    • Dalal, S.1    Kapoor, M.2    Gupta, M.N.3
  • 6
    • 29344453545 scopus 로고    scopus 로고
    • Galacto-oligosaccharide synthesis by immobilized Aspergillus oryzae β-galactosidase
    • Gaur R., Pant H., Jain R., Khare S.K. Galacto-oligosaccharide synthesis by immobilized Aspergillus oryzae β-galactosidase. Food Chem. 2006, 97:426-430.
    • (2006) Food Chem. , vol.97 , pp. 426-430
    • Gaur, R.1    Pant, H.2    Jain, R.3    Khare, S.K.4
  • 7
    • 45249131071 scopus 로고
    • Organic liquids and biocatalysts: theory and practice
    • Halling P.J. Organic liquids and biocatalysts: theory and practice. Trends Biotechnol. 1989, 7:50-52.
    • (1989) Trends Biotechnol. , vol.7 , pp. 50-52
    • Halling, P.J.1
  • 8
    • 51249163381 scopus 로고
    • Salt hydrates possibly suitable for water activity control in organic reaction mixtures for biocatalysis
    • Halling P.J. Salt hydrates possibly suitable for water activity control in organic reaction mixtures for biocatalysis. Biotechnol. Tech. 1992, 6:271-276.
    • (1992) Biotechnol. Tech. , vol.6 , pp. 271-276
    • Halling, P.J.1
  • 9
    • 0014962109 scopus 로고
    • On the structural stability and solvent denaturation of proteins. I. Denaturation by the alcohols and glycols
    • Herskovits T.T., Gadegbeku B., Jaillet H. On the structural stability and solvent denaturation of proteins. I. Denaturation by the alcohols and glycols. J. Biol. Chem. 1970, 245:2588-2598.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2588-2598
    • Herskovits, T.T.1    Gadegbeku, B.2    Jaillet, H.3
  • 11
    • 33845379004 scopus 로고
    • Regioselective oxidation of phenols catalyzed by polyphenol oxidase in chloroform
    • Kazandjian R.Z., Klibanov A.M. Regioselective oxidation of phenols catalyzed by polyphenol oxidase in chloroform. J. Am. Chem. Soc. 1985, 107:5448-5450.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5448-5450
    • Kazandjian, R.Z.1    Klibanov, A.M.2
  • 12
    • 0023385987 scopus 로고
    • Rules for optimization of biocatalysis in organic solvents
    • Laane C., Boeren S., Vos K., Veeger C. Rules for optimization of biocatalysis in organic solvents. Biotechnol. Bioeng. 1987, 30:81-87.
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vos, K.3    Veeger, C.4
  • 13
    • 84855628073 scopus 로고    scopus 로고
    • submitted for publication
    • Specific ion effects of ionic liquids on enzyme activity and stability.
    • Lai, J.-Q., Li, Z., Lü, Y.-H., Yang, Z., submitted for publication. Specific ion effects of ionic liquids on enzyme activity and stability. Green Chem.
    • Green Chem.
    • Lai, J.-Q.1    Li, Z.2    Lü, Y.-H.3    Yang, Z.4
  • 15
    • 0025231704 scopus 로고
    • Sodium dodecyl sulfate activation of a plant polyphenoloxidase
    • Moore B.M., Flurkey W.H. Sodium dodecyl sulfate activation of a plant polyphenoloxidase. J. Biol. Chem. 1990, 265:4982-4988.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4982-4988
    • Moore, B.M.1    Flurkey, W.H.2
  • 16
    • 0344267710 scopus 로고    scopus 로고
    • Improved stability and altered selectivity of tyrosinase based graphite electrodes for detection of phenolic compounds
    • Nistor C., Emnéus J., Gorton L., Ciucu A. Improved stability and altered selectivity of tyrosinase based graphite electrodes for detection of phenolic compounds. Anal. Chim. Acta 1999, 387:309-326.
    • (1999) Anal. Chim. Acta , vol.387 , pp. 309-326
    • Nistor, C.1    Emnéus, J.2    Gorton, L.3    Ciucu, A.4
  • 17
    • 58249132554 scopus 로고    scopus 로고
    • Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase
    • Pchelintsev N.A., Youshko M.I., Švedas V.K. Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase. J. Mol. Catal. B: Enzym. 2009, 56:202-207.
    • (2009) J. Mol. Catal. B: Enzym. , vol.56 , pp. 202-207
    • Pchelintsev, N.A.1    Youshko, M.I.2    Švedas, V.K.3
  • 18
    • 0032031332 scopus 로고    scopus 로고
    • Production of l-DOPA from tyrosinase immobilized on nylon 6,6: enzyme stability and scaleup
    • Pialis P., Saville B.A. Production of l-DOPA from tyrosinase immobilized on nylon 6,6: enzyme stability and scaleup. Enzyme Microb. Technol. 1998, 22:261-268.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 261-268
    • Pialis, P.1    Saville, B.A.2
  • 20
    • 50049088751 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications
    • Sangeetha K., Abraham T.E. Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications. Int. J. Biol. Macromol. 2008, 43:314-319.
    • (2008) Int. J. Biol. Macromol. , vol.43 , pp. 314-319
    • Sangeetha, K.1    Abraham, T.E.2
  • 21
    • 37749006119 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates (CLEA®s): stable and recyclable biocatalysts
    • Sheldon R.A. Cross-linked enzyme aggregates (CLEA®s): stable and recyclable biocatalysts. Biochem. Soc. Trans. 2007, 35:1583-1587.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1583-1587
    • Sheldon, R.A.1
  • 25
    • 18144362501 scopus 로고    scopus 로고
    • Ionic liquids: green solvents for nonaqueous biocatalysis
    • Yang Z., Pan W. Ionic liquids: green solvents for nonaqueous biocatalysis. Enzyme Microb. Technol. 2005, 37:19-28.
    • (2005) Enzyme Microb. Technol. , vol.37 , pp. 19-28
    • Yang, Z.1    Pan, W.2
  • 27
    • 0027897761 scopus 로고
    • Comparison of tyrosinase activity and stability in aqueous and nearly nonaqueous environments
    • Yang Z., Robb D.A. Comparison of tyrosinase activity and stability in aqueous and nearly nonaqueous environments. Enzyme Microb. Technol. 1993, 15:1030-1036.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 1030-1036
    • Yang, Z.1    Robb, D.A.2
  • 28
    • 0028166667 scopus 로고
    • Partition coefficients of substrates and products and solvent selection for biocatalysis under nearly anhydrous conditions
    • Yang Z., Robb D.A. Partition coefficients of substrates and products and solvent selection for biocatalysis under nearly anhydrous conditions. Biotechnol. Bioeng. 1994, 43:365-370.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 365-370
    • Yang, Z.1    Robb, D.A.2
  • 29
    • 0002900642 scopus 로고    scopus 로고
    • Fundamentals of nonaqueous enzymology
    • Blackie Academic & Professional, New York, A.M.P. Koskinen, A.M. Klibanov (Eds.)
    • Yang Z., Russell A.J. Fundamentals of nonaqueous enzymology. Enzymatic Reactions in Organic Media 1996, 43-69. Blackie Academic & Professional, New York. A.M.P. Koskinen, A.M. Klibanov (Eds.).
    • (1996) Enzymatic Reactions in Organic Media , pp. 43-69
    • Yang, Z.1    Russell, A.J.2
  • 30
    • 36649037989 scopus 로고    scopus 로고
    • Tyrosinase activity in ionic liquids
    • Yang Z., Yue Y.-J., Xing M. Tyrosinase activity in ionic liquids. Biotechnol. Lett. 2008, 30:153-158.
    • (2008) Biotechnol. Lett. , vol.30 , pp. 153-158
    • Yang, Z.1    Yue, Y.-J.2    Xing, M.3
  • 31
    • 66549103239 scopus 로고    scopus 로고
    • Importance of the ionic nature of ionic liquids in affecting enzyme performance
    • Yang Z., Yue Y.-J., Huang W.-C., Zhuang X.-M., Chen Z.-T., Xing M. Importance of the ionic nature of ionic liquids in affecting enzyme performance. J. Biochem. 2009, 145(3):355-364.
    • (2009) J. Biochem. , vol.145 , Issue.3 , pp. 355-364
    • Yang, Z.1    Yue, Y.-J.2    Huang, W.-C.3    Zhuang, X.-M.4    Chen, Z.-T.5    Xing, M.6
  • 32
    • 26544458771 scopus 로고    scopus 로고
    • New enzymatic properties in organic media
    • Blackie Academic & Professional, New York, A.M.P. Koskinen, A.M. Klibanov (Eds.)
    • Zaks A. New enzymatic properties in organic media. Enzymatic Reactions in Organic Media 1996, p.70-93. Blackie Academic & Professional, New York. A.M.P. Koskinen, A.M. Klibanov (Eds.).
    • (1996) Enzymatic Reactions in Organic Media , pp. 70-93
    • Zaks, A.1
  • 33
    • 0024287893 scopus 로고
    • The effect of water on enzyme action in organic media
    • Zaks A., Klibanov A.M. The effect of water on enzyme action in organic media. J. Biol. Chem. 1988, 263:8017-8021.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8017-8021
    • Zaks, A.1    Klibanov, A.M.2
  • 34
    • 44649189336 scopus 로고    scopus 로고
    • Resolution of N-(2-ethyl-6-methylphenyl) alanine via cross-linked aggregates of Pseudomonas sp. lipase
    • Zhao L., Zheng L., Gao G., Jia F., Cao S. Resolution of N-(2-ethyl-6-methylphenyl) alanine via cross-linked aggregates of Pseudomonas sp. lipase. J. Mol. Catal. B: Enzym. 2008, 54:7-12.
    • (2008) J. Mol. Catal. B: Enzym. , vol.54 , pp. 7-12
    • Zhao, L.1    Zheng, L.2    Gao, G.3    Jia, F.4    Cao, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.