메뉴 건너뛰기




Volumn 46, Issue 5, 2010, Pages 397-405

Urea degradation kinetics in model wine solutions by acid urease immobilised onto chitosan-derivative beads of different sizes

Author keywords

Chitopearls; Free or immobilised acid urease; Grape seed tannins; Model wine solution; Stirred bioreactor; Urea degradation kinetics

Indexed keywords

DEGRADATION KINETICS; FREE OR IMMOBILISED ACID UREASE; GRAPE SEED TANNINS; GRAPE SEEDS; STIRRED BIOREACTORS;

EID: 77649188638     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.12.010     Document Type: Article
Times cited : (26)

References (39)
  • 1
    • 0000562596 scopus 로고
    • Formation of ethyl carbamate precursors during grape juice (Chardonnay) fermentation. I. Addition of amino acids, urea, and ammonia effects of fortification on intracellular and extracellular precursors
    • Ough C.S., Crowell E.A., Mooney L.A. Formation of ethyl carbamate precursors during grape juice (Chardonnay) fermentation. I. Addition of amino acids, urea, and ammonia effects of fortification on intracellular and extracellular precursors. Am J Enol Viticult 1988, 39:243-249.
    • (1988) Am J Enol Viticult , vol.39 , pp. 243-249
    • Ough, C.S.1    Crowell, E.A.2    Mooney, L.A.3
  • 2
    • 0025304375 scopus 로고
    • The carcinogenic potential of ethyl carbamate (urethane): risk assessment at human dietary exposure levels
    • Schlatter J., Lutz W.K. The carcinogenic potential of ethyl carbamate (urethane): risk assessment at human dietary exposure levels. Food Chem Toxicol 1990, 28:205-211.
    • (1990) Food Chem Toxicol , vol.28 , pp. 205-211
    • Schlatter, J.1    Lutz, W.K.2
  • 3
    • 0003874285 scopus 로고    scopus 로고
    • Food and Drug Administration. Center for Food Safety and Applied Nutrition, Published on line at
    • Butzke C.E., Bisson L.F. Ethyl carbamate preventative action manual 1997, Food and Drug Administration. Center for Food Safety and Applied Nutrition, Published on line at http://www.fda.gov/Food/FoodSafety/FoodContaminantsAdulteration/ChemicalContaminants/EthylCarbamateUrethane/ucm078546.htm.
    • (1997) Ethyl carbamate preventative action manual
    • Butzke, C.E.1    Bisson, L.F.2
  • 4
    • 64649100132 scopus 로고    scopus 로고
    • Functional, catalytic and kinetic properties: a review
    • Krajewska B., Ureases I. Functional, catalytic and kinetic properties: a review. J Mol Catal B: Enzym 2009, 59:9-21.
    • (2009) J Mol Catal B: Enzym , vol.59 , pp. 9-21
    • Krajewska, B.1    Ureases, I.2
  • 5
    • 0013641997 scopus 로고
    • Causes for inhibition of an acid urease from Lactobacillus fermentus
    • Trioli G., Ough C.S. Causes for inhibition of an acid urease from Lactobacillus fermentus. Am J Enol Viticult 1989, 40(4):245-252.
    • (1989) Am J Enol Viticult , vol.40 , Issue.4 , pp. 245-252
    • Trioli, G.1    Ough, C.S.2
  • 6
    • 0024962543 scopus 로고
    • Urea hydrolysis by immobilized urease in a fixed-bed reactor: analysis and kinetic parameter estimation
    • Moynihan H.J., Lee C.K., Clark W., Wang N-H.L. Urea hydrolysis by immobilized urease in a fixed-bed reactor: analysis and kinetic parameter estimation. Biotechnol Bioeng 1989, 34:951-963.
    • (1989) Biotechnol Bioeng , vol.34 , pp. 951-963
    • Moynihan, H.J.1    Lee, C.K.2    Clark, W.3    Wang, N.-H.L.4
  • 7
    • 33748518888 scopus 로고    scopus 로고
    • Assessment of urea degradation rate in model wine solutions by acid urease from Lactobacillus fermentum
    • Fidaleo M., Esti M., Moresi M. Assessment of urea degradation rate in model wine solutions by acid urease from Lactobacillus fermentum. J Agric Food Chem 2006, 54:6226-6235.
    • (2006) J Agric Food Chem , vol.54 , pp. 6226-6235
    • Fidaleo, M.1    Esti, M.2    Moresi, M.3
  • 8
    • 34247194574 scopus 로고    scopus 로고
    • Modeling of urea degradation in white and rosé wines by acid urease
    • Esti M., Fidaleo M., Moresi M., Tamborra P. Modeling of urea degradation in white and rosé wines by acid urease. J Agric Food Chem 2007, 55:2590-2596.
    • (2007) J Agric Food Chem , vol.55 , pp. 2590-2596
    • Esti, M.1    Fidaleo, M.2    Moresi, M.3    Tamborra, P.4
  • 9
    • 0029823022 scopus 로고    scopus 로고
    • Optimal conditions for effective use of acid urease in wine
    • Kodama S. Optimal conditions for effective use of acid urease in wine. J Food Sci 1996, 61(3):548-552.
    • (1996) J Food Sci , vol.61 , Issue.3 , pp. 548-552
    • Kodama, S.1
  • 10
    • 0008605750 scopus 로고
    • Removal of urea from alcoholic beverages by immobilised acid urease
    • Matsumoto K. Removal of urea from alcoholic beverages by immobilised acid urease. Bioprocess Technol 1993, 16:255-273.
    • (1993) Bioprocess Technol , vol.16 , pp. 255-273
    • Matsumoto, K.1
  • 11
    • 43449120393 scopus 로고    scopus 로고
    • Research on orientedly immobilised urease via concanavalin A
    • Zhou J., Chen S., Wang J. Research on orientedly immobilised urease via concanavalin A. Chin J Biotech 2008, 24:617-621.
    • (2008) Chin J Biotech , vol.24 , pp. 617-621
    • Zhou, J.1    Chen, S.2    Wang, J.3
  • 12
    • 54949118377 scopus 로고    scopus 로고
    • A comparative study on immobilisation of urease on different matrices
    • Selvamurugan C., Lavanya A., Sivasankar B. A comparative study on immobilisation of urease on different matrices. J Sci Ind Res 2007, 66:655-659.
    • (2007) J Sci Ind Res , vol.66 , pp. 655-659
    • Selvamurugan, C.1    Lavanya, A.2    Sivasankar, B.3
  • 13
    • 66149143627 scopus 로고    scopus 로고
    • Urea degradation in model wine solutions by free or immobilized acid urease in a stirred bioreactor
    • Andrich L., Esti M., Moresi M. Urea degradation in model wine solutions by free or immobilized acid urease in a stirred bioreactor. J Agric Food Chem 2009, 57:3533-3542.
    • (2009) J Agric Food Chem , vol.57 , pp. 3533-3542
    • Andrich, L.1    Esti, M.2    Moresi, M.3
  • 14
    • 0034274420 scopus 로고    scopus 로고
    • ® C, a carrier for immobilization of enzymes of industrial potential
    • ® C, a carrier for immobilization of enzymes of industrial potential. J Mol Catal B: Enzym 2000, 10:157-176.
    • (2000) J Mol Catal B: Enzym , vol.10 , pp. 157-176
    • Katchalski-Kazir, E.1    Kraemer, D.M.2
  • 15
    • 0036323592 scopus 로고    scopus 로고
    • Eupergit oxirane acrylic beads: how to make enzymes fit for biocatalysis
    • Boller T., Meier C., Menzler S. Eupergit oxirane acrylic beads: how to make enzymes fit for biocatalysis. Org Process Res Dev 2002, 6:509-519.
    • (2002) Org Process Res Dev , vol.6 , pp. 509-519
    • Boller, T.1    Meier, C.2    Menzler, S.3
  • 16
    • 64649100726 scopus 로고    scopus 로고
    • Properties and their customizing by enzyme immobilizations
    • Krajewska B., Ureases I.I. Properties and their customizing by enzyme immobilizations. J Mol Catal B: Enzym 2009, 59:22-40.
    • (2009) J Mol Catal B: Enzym , vol.59 , pp. 22-40
    • Krajewska, B.1    Ureases, I.I.2
  • 17
    • 0032841875 scopus 로고    scopus 로고
    • Preparation and characterization of urease immobilized onto porous chitosan beads for urea hydrolysis
    • Chen J.P., Chiu S.H. Preparation and characterization of urease immobilized onto porous chitosan beads for urea hydrolysis. Bioprocess Eng 1999, 21(4):323-330.
    • (1999) Bioprocess Eng , vol.21 , Issue.4 , pp. 323-330
    • Chen, J.P.1    Chiu, S.H.2
  • 18
    • 63249111145 scopus 로고    scopus 로고
    • Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: analytical applications
    • Kumar S., Dwevedi A., Kayastha A.M. Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: analytical applications. J Mol Catal B: Enzym 2009, 58:138-145.
    • (2009) J Mol Catal B: Enzym , vol.58 , pp. 138-145
    • Kumar, S.1    Dwevedi, A.2    Kayastha, A.M.3
  • 19
    • 0035662771 scopus 로고    scopus 로고
    • Pigeonpea (Cajanus cajan L.) urease immobilized on glutaraldehyde-activated chitosan beads and its analytical applications
    • Kayastha A.M., Srivastava P.K. Pigeonpea (Cajanus cajan L.) urease immobilized on glutaraldehyde-activated chitosan beads and its analytical applications. Appl Biochem Biotechnol 2001, 96:41-53.
    • (2001) Appl Biochem Biotechnol , vol.96 , pp. 41-53
    • Kayastha, A.M.1    Srivastava, P.K.2
  • 20
    • 50649091654 scopus 로고    scopus 로고
    • Tagatose production with pH control in a stirred tank reactor containing immobilized l-arabinose from Thermotoga neapolitana
    • Lim B.-C., Kim H.-J., Oh D.-K. Tagatose production with pH control in a stirred tank reactor containing immobilized l-arabinose from Thermotoga neapolitana. Appl Biochem Biotechnol 2008, 149:245-253.
    • (2008) Appl Biochem Biotechnol , vol.149 , pp. 245-253
    • Lim, B.-C.1    Kim, H.-J.2    Oh, D.-K.3
  • 21
    • 0032211708 scopus 로고    scopus 로고
    • Continuous production of galacto-oligosaccharides from lactose by Bullera singularis β-galactosidase immobilized in chitosan beads
    • Shin H.-J., Park J.-M., Yang J.-W. Continuous production of galacto-oligosaccharides from lactose by Bullera singularis β-galactosidase immobilized in chitosan beads. Process Biochem 1998, 33:787-792.
    • (1998) Process Biochem , vol.33 , pp. 787-792
    • Shin, H.-J.1    Park, J.-M.2    Yang, J.-W.3
  • 22
    • 0343221408 scopus 로고
    • Immobilization of glucoamylase on chitosan beads and application to the conversion of starch to glucose
    • Dhar G.M., Mitsutomi M., Ohtakara A. Immobilization of glucoamylase on chitosan beads and application to the conversion of starch to glucose. Saga Daigaku Nogakubu Iho 1993, 74:59-68.
    • (1993) Saga Daigaku Nogakubu Iho , vol.74 , pp. 59-68
    • Dhar, G.M.1    Mitsutomi, M.2    Ohtakara, A.3
  • 23
    • 0010580403 scopus 로고
    • Determination of l-lactate by differential-pulse polarography with covalently immobilized enzyme on Chitopearl
    • Hasebe K., Hikima S., Yoshida H. Determination of l-lactate by differential-pulse polarography with covalently immobilized enzyme on Chitopearl. Fresenius J Anal Chem 1991, 339:261-263.
    • (1991) Fresenius J Anal Chem , vol.339 , pp. 261-263
    • Hasebe, K.1    Hikima, S.2    Yoshida, H.3
  • 24
    • 0026190157 scopus 로고
    • Immobilization of proteases to porous chitosan beads and their catalysis for ester and peptide synthesis in organic solvents
    • Kise H., Hayakawa A. Immobilization of proteases to porous chitosan beads and their catalysis for ester and peptide synthesis in organic solvents. Enzyme Microb Technol 1991, 13:584-588.
    • (1991) Enzyme Microb Technol , vol.13 , pp. 584-588
    • Kise, H.1    Hayakawa, A.2
  • 25
    • 0034302040 scopus 로고    scopus 로고
    • Mass production of d-psicose from d-fructose by a continuous bioreactor system using immobilized d-tagatose 3-epimerase
    • Takeshita K., Suga A., Takada G., Izumori K. Mass production of d-psicose from d-fructose by a continuous bioreactor system using immobilized d-tagatose 3-epimerase. JBB (J Biosci Bioeng) 2000, 90:453-455.
    • (2000) JBB (J Biosci Bioeng) , vol.90 , pp. 453-455
    • Takeshita, K.1    Suga, A.2    Takada, G.3    Izumori, K.4
  • 26
    • 0028916465 scopus 로고
    • Preparation of d-sorbose from d-tagatose by immobilized d-tagatose 3-epimerase
    • Itoh H., Sato T., Takeuchi T., Khan A.R., Izumori K. Preparation of d-sorbose from d-tagatose by immobilized d-tagatose 3-epimerase. J Ferment Bioeng 1995, 79:184-185.
    • (1995) J Ferment Bioeng , vol.79 , pp. 184-185
    • Itoh, H.1    Sato, T.2    Takeuchi, T.3    Khan, A.R.4    Izumori, K.5
  • 30
    • 0025066281 scopus 로고
    • Immobilisation of chloroperoxidase on aminopropyl-glass
    • Kadima T.A., Pickard M.A. Immobilisation of chloroperoxidase on aminopropyl-glass. Appl Environ Microbiol 1990, 56:3473-3477.
    • (1990) Appl Environ Microbiol , vol.56 , pp. 3473-3477
    • Kadima, T.A.1    Pickard, M.A.2
  • 31
    • 15944399398 scopus 로고    scopus 로고
    • Genetic toxicity and carcinogenicity studies of glutaraldehyde - a review
    • Zeiger E., Gollapudi B., Spencer P. Genetic toxicity and carcinogenicity studies of glutaraldehyde - a review. Mutat Res/Rev Mutat Res 2005, 589:136-151.
    • (2005) Mutat Res/Rev Mutat Res , vol.589 , pp. 136-151
    • Zeiger, E.1    Gollapudi, B.2    Spencer, P.3
  • 35
    • 0009577545 scopus 로고    scopus 로고
    • PH gradients in immobilized amidases and their influence on rates and yields of β-lactam hydrolysis
    • Spieß A., Schlothauer R.-C., Hinrichs J., Scheidat B., Kasche V. pH gradients in immobilized amidases and their influence on rates and yields of β-lactam hydrolysis. Biotechnol Bioeng 1999, 62:267-277.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 267-277
    • Spieß, A.1    Schlothauer, R.-C.2    Hinrichs, J.3    Scheidat, B.4    Kasche, V.5
  • 37
    • 0032047633 scopus 로고    scopus 로고
    • Adsorption of organic acids on polyaminated highly porous chitosan: equilibria
    • Tagatsuji W., Yoshida H. Adsorption of organic acids on polyaminated highly porous chitosan: equilibria. Ind Eng Res 1998, 37:1300-1309.
    • (1998) Ind Eng Res , vol.37 , pp. 1300-1309
    • Tagatsuji, W.1    Yoshida, H.2
  • 38
    • 17344376855 scopus 로고    scopus 로고
    • The rheological properties of Slovenian wines
    • Košmerl T., Abramovič H., Klofutar C. The rheological properties of Slovenian wines. J Food Eng 2000, 46:165-171.
    • (2000) J Food Eng , vol.46 , pp. 165-171
    • Košmerl, T.1    Abramovič, H.2    Klofutar, C.3
  • 39
    • 0002127397 scopus 로고
    • Flow through packed columns
    • Ergun S. Flow through packed columns. Chem Eng Prog 1952, 48:89-94.
    • (1952) Chem Eng Prog , vol.48 , pp. 89-94
    • Ergun, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.