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Volumn 13, Issue 5, 2008, Pages 632-638

Effect of calcium on immobilization of rice (Oryza sativa L.) peroxidase for bioassays in sodium alginate and Agarose gel

Author keywords

Agarose; Alginate; Calcium; Immobilized peroxidase; Oryzasativa; Peroxidase

Indexed keywords

AGAROSE; ALGINIC ACID; CALCIUM ALGINATE; CALCIUM ION; GUAIACOL; HYDROGEN PEROXIDE; PEROXIDASE;

EID: 56849099090     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12257-008-0051-2     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0029109985 scopus 로고
    • Impact of genetic technology on enzyme technology
    • Bickerstaff, G. F. (1995) Impact of genetic technology on enzyme technology. Genet. Engineer. Biotechno. 15: 13-30.
    • (1995) Genet. Engineer. Biotechno. , vol.15 , pp. 13-30
    • Bickerstaff, G.F.1
  • 2
    • 0023949199 scopus 로고
    • Use of Immobilized enzymes in drug metabolism studies
    • Dulik, D. M. and C. Fenselau (1988) Use of Immobilized enzymes in drug metabolism studies. FASEB J. 2: 2235-2240.
    • (1988) FASEB J. , vol.2 , pp. 2235-2240
    • Dulik, D.M.1    Fenselau, C.2
  • 4
    • 0033818431 scopus 로고    scopus 로고
    • Biomedical application of immobilized enzymes
    • Liang, J. F., Y. T. Li, and V. C. Yang (2000) Biomedical application of immobilized enzymes. J. Pharm. Sci. 89: 979-990.
    • (2000) J. Pharm. Sci. , vol.89 , pp. 979-990
    • Liang, J.F.1    Li, Y.T.2    Yang, V.C.3
  • 5
    • 56849104176 scopus 로고    scopus 로고
    • The mode of solidification (immobilization) of plant peroxidases in salt stress as possible recognizing of the changes in their active sites
    • n o 15. July 17-21. Geneva, Switzerland
    • Ginalska, G., J. Lobarzewski, and H. Greppin (1999) The mode of solidification (immobilization) of plant peroxidases in salt stress as possible recognizing of the changes in their active sites. Plant Peroxidase Newsletter n o 15. July 17-21. Geneva, Switzerland.
    • (1999) Plant Peroxidase Newsletter
    • Ginalska, G.1    Lobarzewski, J.2    Greppin, H.3
  • 6
    • 13844266642 scopus 로고    scopus 로고
    • Simultaneous purification and immobilization of bitter gourd (Momordica charantia) peroxidases on bioaffinity support
    • Akhtar, S., A. A. Khan, and Q. Husain (2005) Simultaneous purification and immobilization of bitter gourd (Momordica charantia) peroxidases on bioaffinity support. J. Chem. Technol. Biotechnol. 80: 198-205.
    • (2005) J. Chem. Technol. Biotechnol. , vol.80 , pp. 198-205
    • Akhtar, S.1    Khan, A.A.2    Husain, Q.3
  • 7
    • 0033179684 scopus 로고    scopus 로고
    • Immobilized enzymes: Crystals or carriers
    • Tischer, W. and V. Kasche (1999) Immobilized enzymes: Crystals or carriers. Trends Biotechnol. 17: 326-335.
    • (1999) Trends Biotechnol. , vol.17 , pp. 326-335
    • Tischer, W.1    Kasche, V.2
  • 9
    • 28844472482 scopus 로고    scopus 로고
    • Bioaffinity-based an inexpensive and high yield procedure for the immobilization of turnip (Brassica rapa) peroxidase
    • Kulshrestha, Y. and Q. Husain (2003) Bioaffinity-based an inexpensive and high yield procedure for the immobilization of turnip (Brassica rapa) peroxidase. Enzyme Microb. Technol. 38: 470-477.
    • (2003) Enzyme Microb. Technol. , vol.38 , pp. 470-477
    • Kulshrestha, Y.1    Husain, Q.2
  • 10
    • 0142185232 scopus 로고    scopus 로고
    • Potential use of oxidative enzymes for the detoxification of organic pollutants
    • Torres, E., I. Bustos-Jaimes, and S. Le Borgne (2003) Potential use of oxidative enzymes for the detoxification of organic pollutants. Appl. Catal. B Environ. 46: 1-15.
    • (2003) Appl. Catal. B Environ. , vol.46 , pp. 1-15
    • Torres, E.1    Bustos-Jaimes, I.2    Le Borgne, S.3
  • 11
    • 0034425271 scopus 로고    scopus 로고
    • Detoxification of phenols and aromatic amines from polluted wastewater by using phenol oxidases
    • Husain, Q. and U. Jan (2000) Detoxification of phenols and aromatic amines from polluted wastewater by using phenol oxidases. J. Sci. Ind. Res. 59: 286-293.
    • (2000) J. Sci. Ind. Res. , vol.59 , pp. 286-293
    • Husain, Q.1    Jan, U.2
  • 12
    • 0035809781 scopus 로고    scopus 로고
    • Horseradish peroxidase catalyzed degradation of industrially important dyes
    • Bhunia, A., S. Durani, and P. P. Wangikar (2001) Horseradish peroxidase catalyzed degradation of industrially important dyes. Biotechnol. Bioeng. 72: 562-567.
    • (2001) Biotechnol. Bioeng. , vol.72 , pp. 562-567
    • Bhunia, A.1    Durani, S.2    Wangikar, P.P.3
  • 13
    • 0037010857 scopus 로고    scopus 로고
    • Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: A review
    • Duran, N., M. A. Rosa, A. D'Annibale, and L. Gianfreda (2002) Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: A review. Enzyme Microb. Technol. 31: 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
  • 14
    • 0038348588 scopus 로고    scopus 로고
    • Immobilization of horseradish peroxidase onto polyaniline polymers
    • Fernandes, K. F., C. S. Lima, H. Pinho, and C. H. Collins (2003) Immobilization of horseradish peroxidase onto polyaniline polymers. Process Biochem. 38: 1379-1384.
    • (2003) Process Biochem. , vol.38 , pp. 1379-1384
    • Fernandes, K.F.1    Lima, C.S.2    Pinho, H.3    Collins, C.H.4
  • 15
    • 28844472482 scopus 로고    scopus 로고
    • Direct immobilization of peroxidase on DEAE cellulose from ammonium sulphate fractionated proteins of bitter gourd (Momordica charantia)
    • Kulshrestha, Y. and Q. Husain (2006) Direct immobilization of peroxidase on DEAE cellulose from ammonium sulphate fractionated proteins of bitter gourd (Momordica charantia). Enzyme Microb. Technol. 38: 470-477.
    • (2006) Enzyme Microb. Technol. , vol.38 , pp. 470-477
    • Kulshrestha, Y.1    Husain, Q.2
  • 16
    • 14644393725 scopus 로고    scopus 로고
    • Simultaneous purification and immobilization of mushroom tyrosinase on an immunoaffinity support
    • Khan, A. A., S. Akhtar, and Q. Husain (2005) Simultaneous purification and immobilization of mushroom tyrosinase on an immunoaffinity support. Process Biochem. 40: 2379-2386.
    • (2005) Process Biochem. , vol.40 , pp. 2379-2386
    • Khan, A.A.1    Akhtar, S.2    Husain, Q.3
  • 17
    • 34548602005 scopus 로고    scopus 로고
    • Phytate degradation by immobilized Saccharomyces cerevisiae phytase in soybean-curd whey
    • In, M.-J., K.-H. Kim, and N.-S. Oh (2007) Phytate degradation by immobilized Saccharomyces cerevisiae phytase in soybean-curd whey. Biotechnol. Bioprocess Eng. 12: 348-353.
    • (2007) Biotechnol. Bioprocess Eng. , vol.12 , pp. 348-353
    • In, M.-J.1    Kim, K.-H.2    Oh, N.-S.3
  • 18
    • 0001864081 scopus 로고
    • The water culture method for growing plants without soil
    • Haogland, D. R. and D. I. Arnon (1938) The water culture method for growing plants without soil. Cal. Agric. Exp. Sta. Cir. 3: 346-347.
    • (1938) Cal. Agric. Exp. Sta. Cir. , vol.3 , pp. 346-347
    • Haogland, D.R.1    Arnon, D.I.2
  • 19
    • 0035661857 scopus 로고    scopus 로고
    • Effect of cadmium on lipid peroxidation, superoxide anion generation and activities of antioxidant enzymes in growing rice seedlings
    • Shah, K., R. G. Kumar, S. Verma, and R. S. Dubey (2001) Effect of cadmium on lipid peroxidation, superoxide anion generation and activities of antioxidant enzymes in growing rice seedlings. Plant Sci. 161: 1135-1144.
    • (2001) Plant Sci. , vol.161 , pp. 1135-1144
    • Shah, K.1    Kumar, R.G.2    Verma, S.3    Dubey, R.S.4
  • 21
    • 0000931998 scopus 로고
    • Role of peroxidase in the development of water-impermeable seed coats in Sida spinosa
    • Egley, G. H., R. N. Paul, Jr., K. C. Vaughn, and S. O. Duke (1983) Role of peroxidase in the development of water-impermeable seed coats in Sida spinosa L. Planta 157: 224-232.
    • (1983) L. Planta , vol.157 , pp. 224-232
    • Egley, G.H.1    Paul Jr., R.N.2    Vaughn, K.C.3    Duke, S.O.4
  • 22
    • 0001904122 scopus 로고    scopus 로고
    • Entrapment in calcium alginate
    • In: G. F. Bickerstaff (ed.). Humana Press, Totowa, NJ, USA
    • Fraser, J. E. and G. F. Bickerstaff (1997) Entrapment in calcium alginate. pp. 61-66. In: G. F. Bickerstaff (ed.). Immobilization of Enzymes and Cells. Humana Press, Totowa, NJ, USA.
    • (1997) Immobilization of Enzymes and Cells , pp. 61-66
    • Fraser, J.E.1    Bickerstaff, G.F.2
  • 23
    • 0029140447 scopus 로고
    • Reducing enzyme conformational flexibility by multipoint covalent immobilization
    • Fernandez-Lafuente, R., A. N. P. Wood, and D. A. Cowan (1995) Reducing enzyme conformational flexibility by multipoint covalent immobilization. Biotechnol. Tech. 9: 1-6.
    • (1995) Biotechnol. Tech. , vol.9 , pp. 1-6
    • Fernandez-Lafuente, R.1    Wood, A.N.P.2    Cowan, D.A.3
  • 24
    • 0038235596 scopus 로고    scopus 로고
    • Immobilization of Candida krusei cells producing phytase in alginate gel beads: An application of the preparation of myoinositol phosphatases
    • Quan, C. S., S. D. Fan, and Y. Ohta (2003) Immobilization of Candida krusei cells producing phytase in alginate gel beads: An application of the preparation of myoinositol phosphatases. Appl. Microbiol. Biotechnol. 62: 41-47.
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 41-47
    • Quan, C.S.1    Fan, S.D.2    Ohta, Y.3
  • 25
    • 25844498220 scopus 로고    scopus 로고
    • Physicochemical characterization of watermelon urease upon immobilization in alginate beads
    • Prakash, O. and L. S. B. Upadhyay (2005) Physicochemical characterization of watermelon urease upon immobilization in alginate beads. J. Plant Biochem. Biotechnol. 14: 209-213.
    • (2005) J. Plant Biochem. Biotechnol. , vol.14 , pp. 209-213
    • Prakash, O.1    Upadhyay, L.S.B.2
  • 26
    • 0014462189 scopus 로고
    • Urease covalently coupled to porous glass
    • Weetall, H. H. and L. S. Hersh (1969) Urease covalently coupled to porous glass. Biochim. Biophys. Acta 185: 464-465.
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 464-465
    • Weetall, H.H.1    Hersh, L.S.2
  • 27
    • 0024962543 scopus 로고
    • Urea hydrolysis by immobilized urease in a fixed-bed reactor: Analysis and kinetic parameter estimation
    • Moynihan, H. J., C. K. Lee, W. Clark, and N. H. L. Wang (1989) Urea hydrolysis by immobilized urease in a fixed-bed reactor: Analysis and kinetic parameter estimation. Biotechnol. Bioeng. 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
  • 28
    • 0017248834 scopus 로고
    • Functional groups on enzymes suitable for binding of matrices
    • Srere, P. A. and K. Uyeda (1976) Functional groups on enzymes suitable for binding of matrices. Methods Enzymol. 44: 11-19.
    • (1976) Methods Enzymol. , vol.44 , pp. 11-19
    • Srere, P.A.1    Uyeda, K.2
  • 29
    • 0025983938 scopus 로고
    • Commercially available supports for protein immobilization
    • In: R. F. Taylor (ed.). Marcel Dekker, New York, NY, USA
    • Taylor, R. F. (1991) Commercially available supports for protein immobilization. pp. 139-160. In: R. F. Taylor (ed.). Protein Immobilization. Marcel Dekker, New York, NY, USA.
    • (1991) Protein Immobilization , pp. 139-160
    • Taylor, R.F.1
  • 30
    • 0031036650 scopus 로고    scopus 로고
    • The effect of simultaneous operation of two metal ions on soluble and immobilized peroxidase
    • Brzyska, M., M. Cieszczyk, and J. Lobarzewski (1997) The effect of simultaneous operation of two metal ions on soluble and immobilized peroxidase. J. Chem. Tech. Biotechnol. 68: 101-109.
    • (1997) J. Chem. Tech. Biotechnol. , vol.68 , pp. 101-109
    • Brzyska, M.1    Cieszczyk, M.2    Lobarzewski, J.3
  • 31
    • 34248383717 scopus 로고    scopus 로고
    • Immobilization of watermelon (Citrullus vulgaris) urease in agarose gel for urea estimation
    • Prakash, O., S. Puliga, and L. S. B. Upadhyay (2007) Immobilization of watermelon (Citrullus vulgaris) urease in agarose gel for urea estimation. Biotechnol. Bioprocess Eng. 12: 131-135.
    • (2007) Biotechnol. Bioprocess Eng. , vol.12 , pp. 131-135
    • Prakash, O.1    Puliga, S.2    Upadhyay, L.S.B.3
  • 32
    • 56849106813 scopus 로고    scopus 로고
    • Plant peroxidases - A brief note on response to metal pollutants
    • In: A. Hemantranjan (ed.). Scientific Publishers, Jodhpur, India
    • Shah, K. (2005) Plant peroxidases - a brief note on response to metal pollutants. pp. 113-122. In: A. Hemantranjan (ed.). Advances in Plant Physiology (Molecular Plant Physiology and Biology). Scientific Publishers, Jodhpur, India.
    • (2005) Advances in Plant Physiology (Molecular Plant Physiology and Biology) , pp. 113-122
    • Shah, K.1
  • 33
    • 2942707717 scopus 로고    scopus 로고
    • Immobilization of pigeonpea (Cajanus cajan) urease on DEAE-cellulose paper strips for urea estimation
    • Reddy, K. R. C., P. K. Srivastava, P. M. Dey, and A. M. Kayastha (2004) Immobilization of pigeonpea (Cajanus cajan) urease on DEAE-cellulose paper strips for urea estimation. Biotechnol. Appl. Biochem. 39: 323-327.
    • (2004) Biotechnol. Appl. Biochem. , vol.39 , pp. 323-327
    • Reddy, K.R.C.1    Srivastava, P.K.2    Dey, P.M.3    Kayastha, A.M.4


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