메뉴 건너뛰기




Volumn 14, Issue 3, 2007, Pages 355-362

Stability and decolourization ability of Trametes villosa laccase in liquid ultrasonic fields

Author keywords

Dyes decolourization; Enzyme stability; Protein aggregation; Sonochemistry; Ultrasound

Indexed keywords

CAVITATION; DYES; EFFLUENTS; POLYVINYL ALCOHOLS; SONOCHEMISTRY; ULTRASONICS;

EID: 37849187981     PISSN: 13504177     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ultsonch.2006.07.005     Document Type: Article
Times cited : (87)

References (45)
  • 1
    • 37949024622 scopus 로고    scopus 로고
    • P. Sørup, C. Tils, O. Wolf, IPTS study, in: P. Sørup, C. Tils, O. Wolf (Eds.), Biocatalysis: state of the art in Europe, Institute for prospective technological studies (IPTS), Sevilla, Spain, 1998, p. 61.
  • 2
    • 13644282658 scopus 로고    scopus 로고
    • Ultrasound in textile dyeing and the decolourization/mineralization of textile dyes
    • Vajnhandl S., and Le Marechal A.M. Ultrasound in textile dyeing and the decolourization/mineralization of textile dyes. Dyes and Pigments 65 (2005) 89-101
    • (2005) Dyes and Pigments , vol.65 , pp. 89-101
    • Vajnhandl, S.1    Le Marechal, A.M.2
  • 3
    • 0037348953 scopus 로고    scopus 로고
    • Studies on the use of power ultrasound in leather dyeing
    • Sivakumar V., and Rao P.G. Studies on the use of power ultrasound in leather dyeing. Ultrasonics Sonochemistry 10 (2003) 85-94
    • (2003) Ultrasonics Sonochemistry , vol.10 , pp. 85-94
    • Sivakumar, V.1    Rao, P.G.2
  • 4
    • 13644278812 scopus 로고    scopus 로고
    • Ultrasonic assisted dyeing: III. Dyeing of wool with lac as a natural dye
    • Kamel M.M., El-Shishtawy R.M., Yussef B.M., and Mashaly H. Ultrasonic assisted dyeing: III. Dyeing of wool with lac as a natural dye. Dyes and Pigments 65 (2005) 103-110
    • (2005) Dyes and Pigments , vol.65 , pp. 103-110
    • Kamel, M.M.1    El-Shishtawy, R.M.2    Yussef, B.M.3    Mashaly, H.4
  • 7
    • 1642617392 scopus 로고    scopus 로고
    • Use of ultrasonic energy for intensification of the bio-preparation of greige cotton
    • Yachmenev V.G., Blanchard E.J., and Lambert A.H. Use of ultrasonic energy for intensification of the bio-preparation of greige cotton. Ultrasonics 42 (2004) 87-91
    • (2004) Ultrasonics , vol.42 , pp. 87-91
    • Yachmenev, V.G.1    Blanchard, E.J.2    Lambert, A.H.3
  • 8
    • 3142776187 scopus 로고    scopus 로고
    • Intensification of mass transfer in wet textile processes by power ultrasound
    • Moholkar V.S., Nierstrasz V.A., and Warmoeskerken M.M.C.G. Intensification of mass transfer in wet textile processes by power ultrasound. AUTEX Research Journal 3 3 (2003) 129-138
    • (2003) AUTEX Research Journal , vol.3 , Issue.3 , pp. 129-138
    • Moholkar, V.S.1    Nierstrasz, V.A.2    Warmoeskerken, M.M.C.G.3
  • 9
    • 1042268069 scopus 로고    scopus 로고
    • Mechanism of mass-transfer enhancement in textiles by ultrasound
    • Moholkar V.S., and Warmoeskerken M.M.C.G. Mechanism of mass-transfer enhancement in textiles by ultrasound. AIChE Journal 50 1 (2004) 58-64
    • (2004) AIChE Journal , vol.50 , Issue.1 , pp. 58-64
    • Moholkar, V.S.1    Warmoeskerken, M.M.C.G.2
  • 13
    • 0037106452 scopus 로고    scopus 로고
    • S-S bonds are not required for the sonochemical formation of proteinaceous microspheres: the case of streptavidin
    • Avivi S., and Gedanken A. S-S bonds are not required for the sonochemical formation of proteinaceous microspheres: the case of streptavidin. Biochemical Journal 366 (2002) 705-707
    • (2002) Biochemical Journal , vol.366 , pp. 705-707
    • Avivi, S.1    Gedanken, A.2
  • 14
    • 10044243679 scopus 로고    scopus 로고
    • The preparation of avidin microspheres using the sonochemical method and the interaction of the microspheres with biotin
    • Avivi S., and Gedanken A. The preparation of avidin microspheres using the sonochemical method and the interaction of the microspheres with biotin. Ultrasonics Sonochemistry 12 (2005) 405-409
    • (2005) Ultrasonics Sonochemistry , vol.12 , pp. 405-409
    • Avivi, S.1    Gedanken, A.2
  • 15
    • 32944482033 scopus 로고    scopus 로고
    • Interfacial properties and structural conformation of thermosonicated bovine serum albumin
    • Güzey D., Gülseren I., Bruce B., and Weiss J. Interfacial properties and structural conformation of thermosonicated bovine serum albumin. Food Hydrocolloids 20 (2006) 669-677
    • (2006) Food Hydrocolloids , vol.20 , pp. 669-677
    • Güzey, D.1    Gülseren, I.2    Bruce, B.3    Weiss, J.4
  • 16
    • 23744458964 scopus 로고    scopus 로고
    • Ultrasound-accelerated enzymatic synthesis of sugar esters in nonaqueous solvents
    • Xiao Y., Wu Q., Cai Y., and Lin X. Ultrasound-accelerated enzymatic synthesis of sugar esters in nonaqueous solvents. Carbohydrate Research 340 (2005) 2097-2103
    • (2005) Carbohydrate Research , vol.340 , pp. 2097-2103
    • Xiao, Y.1    Wu, Q.2    Cai, Y.3    Lin, X.4
  • 18
    • 4043165652 scopus 로고    scopus 로고
    • Effects of ultrasound and additives on the function and structure of trypsin
    • Tian Z.M., Wan M.X., Wang S.P., and Kang J.Q. Effects of ultrasound and additives on the function and structure of trypsin. Ultrasonics Sonochemistry 11 (2004) 399-404
    • (2004) Ultrasonics Sonochemistry , vol.11 , pp. 399-404
    • Tian, Z.M.1    Wan, M.X.2    Wang, S.P.3    Kang, J.Q.4
  • 19
    • 0032669502 scopus 로고    scopus 로고
    • The use of ultrasound in food technology I: Inactivation of peroxidase by thermosonication
    • De Gennaro L., Cavella S., Romano R., and Masi P. The use of ultrasound in food technology I: Inactivation of peroxidase by thermosonication. Journal of Food Engineering 39 (1999) 401-407
    • (1999) Journal of Food Engineering , vol.39 , pp. 401-407
    • De Gennaro, L.1    Cavella, S.2    Romano, R.3    Masi, P.4
  • 20
    • 0034042912 scopus 로고    scopus 로고
    • The stability of enzymes after sonication
    • Özbek B., and Ülgen K.O. The stability of enzymes after sonication. Process Biochemistry 35 (2000) 1037-1043
    • (2000) Process Biochemistry , vol.35 , pp. 1037-1043
    • Özbek, B.1    Ülgen, K.O.2
  • 21
    • 0342679110 scopus 로고    scopus 로고
    • The effects of ultrasound on the activities of some glycosidase enzymes of industrial importance
    • Barton S., Bullock C., and Weir D. The effects of ultrasound on the activities of some glycosidase enzymes of industrial importance. Enzyme and Microbial Technology 18 (1996) 190-194
    • (1996) Enzyme and Microbial Technology , vol.18 , pp. 190-194
    • Barton, S.1    Bullock, C.2    Weir, D.3
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantisation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantisation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0028501285 scopus 로고
    • Dosimetry in sonochemistry: The use of aqueous terephthalate ion as a fluorescence monitor
    • Mason T.J., Lorimer J.P., Bates D.M., and Zhao Y. Dosimetry in sonochemistry: The use of aqueous terephthalate ion as a fluorescence monitor. Ultrasonics Sonochemistry 1 2 (1994) 91-95
    • (1994) Ultrasonics Sonochemistry , vol.1 , Issue.2 , pp. 91-95
    • Mason, T.J.1    Lorimer, J.P.2    Bates, D.M.3    Zhao, Y.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriofage-T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriofage-T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0030196117 scopus 로고    scopus 로고
    • Sonochemical degradation of carbon tetrachloride in aqueous solution at two frequencies: 20 kHz and 500 kHz
    • Francony A., and Pétrier C. Sonochemical degradation of carbon tetrachloride in aqueous solution at two frequencies: 20 kHz and 500 kHz. Ultrasonics Sonochemistry 3 (1996) 77-82
    • (1996) Ultrasonics Sonochemistry , vol.3 , pp. 77-82
    • Francony, A.1    Pétrier, C.2
  • 27
    • 0031240131 scopus 로고    scopus 로고
    • Ultrasonic waste-water treatment: Incidence of ultrasonic frequency on the rate of phenol and carbon tetrachloride degradation
    • Pétrier C., and Francony A. Ultrasonic waste-water treatment: Incidence of ultrasonic frequency on the rate of phenol and carbon tetrachloride degradation. Ultrasonics Sonochemistry 4 (1997) 295-300
    • (1997) Ultrasonics Sonochemistry , vol.4 , pp. 295-300
    • Pétrier, C.1    Francony, A.2
  • 28
    • 0029929440 scopus 로고    scopus 로고
    • Ultrasonic degradation at 20 kHz and 500 kHz of atrazine and pentachlorophenol in aqueous solution: preliminary results
    • Pétrier C., David B., and Laguian S. Ultrasonic degradation at 20 kHz and 500 kHz of atrazine and pentachlorophenol in aqueous solution: preliminary results. Chemosphere 32 9 (1996) 1709-1718
    • (1996) Chemosphere , vol.32 , Issue.9 , pp. 1709-1718
    • Pétrier, C.1    David, B.2    Laguian, S.3
  • 29
    • 33646536038 scopus 로고    scopus 로고
    • Sonolysis of 4-chlorophenol in aqueous solution: Effects of substrate concentration, aqueous temperature and ultrasonic frequency
    • Jiang Y., Pétrier C., and Waite T.D. Sonolysis of 4-chlorophenol in aqueous solution: Effects of substrate concentration, aqueous temperature and ultrasonic frequency. Ultrasonics Sonochemistry 13 (2006) 415-422
    • (2006) Ultrasonics Sonochemistry , vol.13 , pp. 415-422
    • Jiang, Y.1    Pétrier, C.2    Waite, T.D.3
  • 30
    • 11944266273 scopus 로고    scopus 로고
    • The PVA solution structure-change effect for α-amylase specific activation
    • Takada T., and Hirai T. The PVA solution structure-change effect for α-amylase specific activation. Polymer Bulletin 53 (2004) 63-71
    • (2004) Polymer Bulletin , vol.53 , pp. 63-71
    • Takada, T.1    Hirai, T.2
  • 31
    • 1142305995 scopus 로고    scopus 로고
    • Stabilization of chloroperoxidase by polyethylene glycols in aqueous media: kinetic studies and synthetic applications
    • Spreti N., Germani R., Incani A., and Savelli G. Stabilization of chloroperoxidase by polyethylene glycols in aqueous media: kinetic studies and synthetic applications. Biotechnology Progress 20 1 (2004) 96-101
    • (2004) Biotechnology Progress , vol.20 , Issue.1 , pp. 96-101
    • Spreti, N.1    Germani, R.2    Incani, A.3    Savelli, G.4
  • 32
    • 0033968970 scopus 로고    scopus 로고
    • Treatment of aqueous phenol with soybean peroxidase in the presence of polyethylene glycol
    • Kinsley C., and Nicell J.A. Treatment of aqueous phenol with soybean peroxidase in the presence of polyethylene glycol. Bioresource Technology 73 (2000) 139-146
    • (2000) Bioresource Technology , vol.73 , pp. 139-146
    • Kinsley, C.1    Nicell, J.A.2
  • 33
    • 0032843986 scopus 로고    scopus 로고
    • Removal of phenolic compounds from synthetic wastewater using soybean peroxidase
    • Caza N., Bewtra J.K., Biswas N., and Taylor K.E. Removal of phenolic compounds from synthetic wastewater using soybean peroxidase. Water Research 33 13 (1999) 3012-3018
    • (1999) Water Research , vol.33 , Issue.13 , pp. 3012-3018
    • Caza, N.1    Bewtra, J.K.2    Biswas, N.3    Taylor, K.E.4
  • 34
    • 27544458645 scopus 로고    scopus 로고
    • Laccase-catalysed removal of bisphenol-A from water: protective effect of PEG on enzyme activity
    • Modaressi K., Taylor K.E., Bewtra J.K., and Biswas N. Laccase-catalysed removal of bisphenol-A from water: protective effect of PEG on enzyme activity. Water Research 39 (2005) 4309-4316
    • (2005) Water Research , vol.39 , pp. 4309-4316
    • Modaressi, K.1    Taylor, K.E.2    Bewtra, J.K.3    Biswas, N.4
  • 35
    • 0037416761 scopus 로고    scopus 로고
    • Laccase-catalysed oxidation of naphthol in the presence of soluble polymers
    • Kulys J., Vidziunaite R., and Schneider P. Laccase-catalysed oxidation of naphthol in the presence of soluble polymers. Enzyme and Microbial Technology 32 (2003) 455-463
    • (2003) Enzyme and Microbial Technology , vol.32 , pp. 455-463
    • Kulys, J.1    Vidziunaite, R.2    Schneider, P.3
  • 36
    • 16644378605 scopus 로고    scopus 로고
    • Disulphide bond formation in food protein aggregation and gelation
    • Visschers R.W., and de Jongh H.H.J. Disulphide bond formation in food protein aggregation and gelation. Biotechnology Advances 23 (2005) 75-80
    • (2005) Biotechnology Advances , vol.23 , pp. 75-80
    • Visschers, R.W.1    de Jongh, H.H.J.2
  • 37
    • 37949038644 scopus 로고    scopus 로고
    • www.expasy.org/sprot.
  • 38
    • 4344636825 scopus 로고    scopus 로고
    • Low frequency ultrasound induces aggregation of porcine fumarase by free radicals production
    • Barteri M., Diociaiuti M., Pala A., and Rotella S. Low frequency ultrasound induces aggregation of porcine fumarase by free radicals production. Biophysical Chemistry 111 (2004) 35-42
    • (2004) Biophysical Chemistry , vol.111 , pp. 35-42
    • Barteri, M.1    Diociaiuti, M.2    Pala, A.3    Rotella, S.4
  • 41
    • 2942735047 scopus 로고    scopus 로고
    • Stainless steel sponge: A novel carrier for the immobilisation of the white-rot fungus Trametes hirsuta for decolourization of textile dyes
    • Couto S.R., Sanromán M.A., Hofer D., and Gübitz G.M. Stainless steel sponge: A novel carrier for the immobilisation of the white-rot fungus Trametes hirsuta for decolourization of textile dyes. Bioresource Technology 95 (2004) 67-72
    • (2004) Bioresource Technology , vol.95 , pp. 67-72
    • Couto, S.R.1    Sanromán, M.A.2    Hofer, D.3    Gübitz, G.M.4
  • 42
    • 17444419429 scopus 로고    scopus 로고
    • Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes
    • Camarero S., Ibarra D., Martínez M.J., and Martínez A.T. Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes. Applied and Environmental Microbiology 71 4 (2005) 1775-1784
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.4 , pp. 1775-1784
    • Camarero, S.1    Ibarra, D.2    Martínez, M.J.3    Martínez, A.T.4
  • 43
    • 6344260152 scopus 로고    scopus 로고
    • Sonochemical degradation of azo dyes in aqueous solution: A new heterogeneous kinetics model taking into account the local concentration of OH radicals and azo dyes
    • Okitsu K., Iwasaki K., Yobiko Y., Bandow H., Nishimura R., and Maeda Y. Sonochemical degradation of azo dyes in aqueous solution: A new heterogeneous kinetics model taking into account the local concentration of OH radicals and azo dyes. Ultrasonics Sonochemistry 12 (2005) 255-262
    • (2005) Ultrasonics Sonochemistry , vol.12 , pp. 255-262
    • Okitsu, K.1    Iwasaki, K.2    Yobiko, Y.3    Bandow, H.4    Nishimura, R.5    Maeda, Y.6
  • 44
    • 1642601665 scopus 로고    scopus 로고
    • Individual combined effects of ultrasound, ozone and UV irradiation: a case study with textile dyes
    • Tezcanli-Güyer G., and Ince N.H. Individual combined effects of ultrasound, ozone and UV irradiation: a case study with textile dyes. Ultrasonics 42 (2004) 603-609
    • (2004) Ultrasonics , vol.42 , pp. 603-609
    • Tezcanli-Güyer, G.1    Ince, N.H.2
  • 45
    • 1842685238 scopus 로고    scopus 로고
    • Application of power ultrasound for azo dye degradation
    • Rehorek A., Tauber M., and Gübitz G. Application of power ultrasound for azo dye degradation. Ultrasonics Sonochemistry 11 (2004) 177-182
    • (2004) Ultrasonics Sonochemistry , vol.11 , pp. 177-182
    • Rehorek, A.1    Tauber, M.2    Gübitz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.