메뉴 건너뛰기




Volumn 102, Issue 20, 2011, Pages 9360-9367

Activity stabilization of Aspergillus niger and Escherichia coli phytases immobilized on allophanic synthetic compounds and montmorillonite nanoclays

Author keywords

Enzyme immobilization; Nanoclay; Phosphorus; Phytase; Phytate

Indexed keywords

ACIDIC CONDITIONS; ACTIVATION ENTHALPIES; ACTIVITY STABILIZATION; ASPERGILLUS NIGER; E. COLI; FREE ENZYME; NANO CLAYS; NANOCLAY; NATURAL MONTMORILLONITE; NIGER; OPTIMAL CONDITIONS; PH VALUE; PHYTASE ACTIVITY; PHYTASES; PHYTATE; RESIDUAL ACTIVITY; SOLID SUPPORTS; SYNTHETIC COMPOUNDS;

EID: 80052762812     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2011.07.054     Document Type: Article
Times cited : (69)

References (37)
  • 1
    • 15344339081 scopus 로고    scopus 로고
    • Application of natural kaolin as support for the immobilization of lipase from Candida rugosa as biocatalyst for effective esterification
    • Abdul Rahman M., Tajudin S., Hussein M., Abdul Rahman R., Salleh A., Basri M. Application of natural kaolin as support for the immobilization of lipase from Candida rugosa as biocatalyst for effective esterification. Applied Clay Science 2005, 29(2):111-116.
    • (2005) Applied Clay Science , vol.29 , Issue.2 , pp. 111-116
    • Abdul Rahman, M.1    Tajudin, S.2    Hussein, M.3    Abdul Rahman, R.4    Salleh, A.5    Basri, M.6
  • 2
    • 77953226231 scopus 로고    scopus 로고
    • Degradation of polycyclic aromatic hydrocarbons by free and nanoclay-immobilized manganese peroxidase from Anthracophyllum discolor
    • Acevedo F., Pizzul L., Castillo M., González M., Cea M., Gianfreda L., Diez M. Degradation of polycyclic aromatic hydrocarbons by free and nanoclay-immobilized manganese peroxidase from Anthracophyllum discolor. Chemosphere 2010, 80:271-278.
    • (2010) Chemosphere , vol.80 , pp. 271-278
    • Acevedo, F.1    Pizzul, L.2    Castillo, M.3    González, M.4    Cea, M.5    Gianfreda, L.6    Diez, M.7
  • 3
    • 0023468837 scopus 로고
    • Protein adsorption and materials biocompatibility: a tutorial review and suggested hypotheses
    • Andrade J., Hlady V. Protein adsorption and materials biocompatibility: a tutorial review and suggested hypotheses. Biopolymers 1986, 79:1-63.
    • (1986) Biopolymers , vol.79 , pp. 1-63
    • Andrade, J.1    Hlady, V.2
  • 4
    • 77958168683 scopus 로고    scopus 로고
    • Immobilization of intracellular carbonyl reductase from Geotrichum candidum for the stereoselective reduction of 1-naphthyl ketone
    • Bhattacharyya M.S., Singh A., Banerjee U. Immobilization of intracellular carbonyl reductase from Geotrichum candidum for the stereoselective reduction of 1-naphthyl ketone. Bioresource technology 2010, 101(6):1581-1586.
    • (2010) Bioresource technology , vol.101 , Issue.6 , pp. 1581-1586
    • Bhattacharyya, M.S.1    Singh, A.2    Banerjee, U.3
  • 6
    • 77249128535 scopus 로고    scopus 로고
    • Natural nanoclays: applications and future trends - a Chilean perspective
    • Calabi-Floody M., Theng B., Reyes P., Mora M. Natural nanoclays: applications and future trends - a Chilean perspective. Clay Minerals 2009, 44(2):161.
    • (2009) Clay Minerals , vol.44 , Issue.2 , pp. 161
    • Calabi-Floody, M.1    Theng, B.2    Reyes, P.3    Mora, M.4
  • 7
    • 75549090824 scopus 로고
    • Síntesis de aluminosilicatos semejantes a los existentes en suelos volcanicos
    • Díaz P., Galindo G., Escudey M. Síntesis de aluminosilicatos semejantes a los existentes en suelos volcanicos. Boletin de la Sociedad Chilena de Quimica 1990, 35:385-389.
    • (1990) Boletin de la Sociedad Chilena de Quimica , vol.35 , pp. 385-389
    • Díaz, P.1    Galindo, G.2    Escudey, M.3
  • 8
    • 0000032025 scopus 로고
    • Total surface of clays in polar liquids as a characteristic index
    • Dyal R., Hendricks S. Total surface of clays in polar liquids as a characteristic index. Soil Science 1950, 69(6):503.
    • (1950) Soil Science , vol.69 , Issue.6 , pp. 503
    • Dyal, R.1    Hendricks, S.2
  • 9
    • 33845588953 scopus 로고    scopus 로고
    • Differential interaction of Aspergillus niger and Peniophora lycii phytases with soil particles affects the hydrolysis of inositol phosphates
    • George T.S., Simpson R.J., Gregory P.J., Richardson A.E. Differential interaction of Aspergillus niger and Peniophora lycii phytases with soil particles affects the hydrolysis of inositol phosphates. Soil Biology and Biochemistry 2007, 39(3):793-803.
    • (2007) Soil Biology and Biochemistry , vol.39 , Issue.3 , pp. 793-803
    • George, T.S.1    Simpson, R.J.2    Gregory, P.J.3    Richardson, A.E.4
  • 10
    • 0030592120 scopus 로고    scopus 로고
    • Construction of a bioreactor to produce special breakdown products of phytate
    • Greiner R., Konietzny U. Construction of a bioreactor to produce special breakdown products of phytate. Journal of Biotechnology 1996, 48(1-2):153-159.
    • (1996) Journal of Biotechnology , vol.48 , Issue.1-2 , pp. 153-159
    • Greiner, R.1    Konietzny, U.2
  • 11
    • 0027208581 scopus 로고
    • Purification and characterization of two phytases from Escherichia coli
    • Greiner R., Konietzny U., Jany K. Purification and characterization of two phytases from Escherichia coli. Archives of Biochemistry and Biophysics 1993, 303(1):107-113.
    • (1993) Archives of Biochemistry and Biophysics , vol.303 , Issue.1 , pp. 107-113
    • Greiner, R.1    Konietzny, U.2    Jany, K.3
  • 12
    • 46949100881 scopus 로고    scopus 로고
    • Production of D-myo-inositol (1,2,4,5,6) pentakisphosphate using alginate-entrapped recombinant Pantoea agglomerans glucose-1-phosphatase
    • Greiner R., Sajidan A. Production of D-myo-inositol (1,2,4,5,6) pentakisphosphate using alginate-entrapped recombinant Pantoea agglomerans glucose-1-phosphatase. Brazil Arch. Biol. Technol. 2008, 51:235-246.
    • (2008) Brazil Arch. Biol. Technol. , vol.51 , pp. 235-246
    • Greiner, R.1    Sajidan, A.2
  • 13
    • 34548602005 scopus 로고    scopus 로고
    • Phytate degradation by immobilized Saccharomyces cerevisiae phytase in soybean-curd whey
    • In M., Kim K., Oh N. Phytate degradation by immobilized Saccharomyces cerevisiae phytase in soybean-curd whey. Biotechnology and Bioprocess Engineering 2007, 12(4):348-353.
    • (2007) Biotechnology and Bioprocess Engineering , vol.12 , Issue.4 , pp. 348-353
    • In, M.1    Kim, K.2    Oh, N.3
  • 14
    • 0036392241 scopus 로고    scopus 로고
    • Molecular and catalytic properties of phytate degrading enzymes (phytases)
    • Konietzny U., Greiner R. Molecular and catalytic properties of phytate degrading enzymes (phytases). International Journal of Food Science & Technology 2002, 37(7):791-812.
    • (2002) International Journal of Food Science & Technology , vol.37 , Issue.7 , pp. 791-812
    • Konietzny, U.1    Greiner, R.2
  • 15
    • 0033591464 scopus 로고    scopus 로고
    • Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4Å resolution1
    • Kostrewa D., Wyss M., D'Arcy A., van Loon A. Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4Å resolution1. Journal of Molecular Biology 1999, 288(5):965-974.
    • (1999) Journal of Molecular Biology , vol.288 , Issue.5 , pp. 965-974
    • Kostrewa, D.1    Wyss, M.2    D'Arcy, A.3    van Loon, A.4
  • 17
    • 0030404756 scopus 로고    scopus 로고
    • Extracellular enzyme activity in soil: effect of pH and ionic strength on the interaction with montmorillonite of two acid phosphatases secreted by the ectomycorrhizal fungus Hebeloma cylindrosporum
    • Leprince F., Quiquampoix H. Extracellular enzyme activity in soil: effect of pH and ionic strength on the interaction with montmorillonite of two acid phosphatases secreted by the ectomycorrhizal fungus Hebeloma cylindrosporum. European Journal of Soil Science 1996, 47(4):511-522.
    • (1996) European Journal of Soil Science , vol.47 , Issue.4 , pp. 511-522
    • Leprince, F.1    Quiquampoix, H.2
  • 18
    • 0033952704 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli phytase and its complex with phytate
    • Lim D., Golovan S., Forsberg C., Jia Z. Crystal structures of Escherichia coli phytase and its complex with phytate. Nature Structural & Molecular Biology 2000, 7(2):108-113.
    • (2000) Nature Structural & Molecular Biology , vol.7 , Issue.2 , pp. 108-113
    • Lim, D.1    Golovan, S.2    Forsberg, C.3    Jia, Z.4
  • 19
    • 0033198351 scopus 로고    scopus 로고
    • Effect of immobilization on pH and thermal stability of Aspergillus ficuum phytase
    • Liu B., Jong C., Tzeng Y. Effect of immobilization on pH and thermal stability of Aspergillus ficuum phytase. Enzyme and Microbial Technology 1999, 25(6):517-521.
    • (1999) Enzyme and Microbial Technology , vol.25 , Issue.6 , pp. 517-521
    • Liu, B.1    Jong, C.2    Tzeng, Y.3
  • 21
    • 75549083950 scopus 로고
    • Sintesis, caracterizacion y reactividad de un suelo alofanico modelo,
    • Doctor, USACH. Santiago
    • Mora, M. 1992. Sintesis, caracterizacion y reactividad de un suelo alofanico modelo, Vol. Doctor, USACH. Santiago, pp. 125.
    • (1992) , pp. 125
    • Mora, M.1
  • 25
    • 80052733877 scopus 로고    scopus 로고
    • Protein adsorption at solid surfaces and protein complexation with humic acids
    • Norde W., Tan W., Koopal L. Protein adsorption at solid surfaces and protein complexation with humic acids. Journal of Soil Science and Plant Nutrition 2008, 8(3):64-74.
    • (2008) Journal of Soil Science and Plant Nutrition , vol.8 , Issue.3 , pp. 64-74
    • Norde, W.1    Tan, W.2    Koopal, L.3
  • 26
    • 77249167826 scopus 로고    scopus 로고
    • Allophane and imogolite: role in soil biogeochemical processes
    • Parfitt R. Allophane and imogolite: role in soil biogeochemical processes. Clay Minerals 2009, 44(1):135.
    • (2009) Clay Minerals , vol.44 , Issue.1 , pp. 135
    • Parfitt, R.1
  • 27
    • 77953206645 scopus 로고    scopus 로고
    • Interaction with soil constituents determines the environmental impact of proteins
    • Quiquampoix H. Interaction with soil constituents determines the environmental impact of proteins. Journal of Soil Science and Plant Nutrition 2008, 8:75-83.
    • (2008) Journal of Soil Science and Plant Nutrition , vol.8 , pp. 75-83
    • Quiquampoix, H.1
  • 28
    • 70349232776 scopus 로고    scopus 로고
    • Molecular characterization, physicochemical properties, known and potential applications of phytases: an overview
    • Rao D., Rao K., Reddy T., Reddy V. Molecular characterization, physicochemical properties, known and potential applications of phytases: an overview. Critical Reviews in Biotechnology 2009, 29(2):182-198.
    • (2009) Critical Reviews in Biotechnology , vol.29 , Issue.2 , pp. 182-198
    • Rao, D.1    Rao, K.2    Reddy, T.3    Reddy, V.4
  • 29
    • 0033923718 scopus 로고    scopus 로고
    • Interaction of acid phosphatase with clays, organic molecules and organo-mineral complexes: kinetics and stability
    • Rao M., Violante A., Gianfreda L. Interaction of acid phosphatase with clays, organic molecules and organo-mineral complexes: kinetics and stability. Soil Biology and Biochemistry 2000, 32(7):1007-1014.
    • (2000) Soil Biology and Biochemistry , vol.32 , Issue.7 , pp. 1007-1014
    • Rao, M.1    Violante, A.2    Gianfreda, L.3
  • 30
    • 43849112802 scopus 로고    scopus 로고
    • Catalytic behaviour of acid phosphatase immobilized on natural supports in the presence of manganese or molybdenum
    • Rosas A., z Mora M., Jara A., López R., Rao M., Gianfreda L. Catalytic behaviour of acid phosphatase immobilized on natural supports in the presence of manganese or molybdenum. Geoderma 2008, 145(1-2):77-83.
    • (2008) Geoderma , vol.145 , Issue.1-2 , pp. 77-83
    • Rosas, A.1    z Mora, M.2    Jara, A.3    López, R.4    Rao, M.5    Gianfreda, L.6
  • 32
    • 85102225009 scopus 로고    scopus 로고
    • Interactions of enzymes with clays and applications in bioremediation
    • Soil Science Society of America, Madison, J.B. Dixon, D.G. Schulze (Eds.)
    • Shen S., Tu S., Taylor R. Interactions of enzymes with clays and applications in bioremediation. Soil Mineralogy with Environmental Applications 2002, 795-818. Soil Science Society of America, Madison. J.B. Dixon, D.G. Schulze (Eds.).
    • (2002) Soil Mineralogy with Environmental Applications , pp. 795-818
    • Shen, S.1    Tu, S.2    Taylor, R.3
  • 34
    • 80052701250 scopus 로고    scopus 로고
    • Enzymes for Industrial Applications (BIO030E). BCC RESEARCH.
    • Thakore, Y. 2008. Enzymes for Industrial Applications (BIO030E). BCC RESEARCH.
    • (2008)
    • Thakore, Y.1
  • 35
    • 0035809040 scopus 로고    scopus 로고
    • Modeling the effect of temperature and pH on activity of enzymes: the case of phytases
    • Tijskens L., Greiner R., Biekman E., Konietzny U. Modeling the effect of temperature and pH on activity of enzymes: the case of phytases. Biotechnology and Bioengineering 2001, 72(3):323-330.
    • (2001) Biotechnology and Bioengineering , vol.72 , Issue.3 , pp. 323-330
    • Tijskens, L.1    Greiner, R.2    Biekman, E.3    Konietzny, U.4
  • 36
    • 0024181017 scopus 로고
    • Aspergillus ficuum extracellular phytase: immobilization on glutaraldehyde-activated silicate
    • Ullah A., Cummins B. Aspergillus ficuum extracellular phytase: immobilization on glutaraldehyde-activated silicate. Annals of the New York Academy of Sciences 1988, 542:102-106.
    • (1988) Annals of the New York Academy of Sciences , vol.542 , pp. 102-106
    • Ullah, A.1    Cummins, B.2
  • 37
    • 22844451738 scopus 로고    scopus 로고
    • Use of phytases (myo-inositolhexakisphosphate phosphohydrolases) for combatting environmental pollution: a biological approach
    • Vats P., Bhattacharyya M.S., Banerjee U.C. Use of phytases (myo-inositolhexakisphosphate phosphohydrolases) for combatting environmental pollution: a biological approach. Critical Reviews in Environmental Science and Technology 2005, 35(5):469-486.
    • (2005) Critical Reviews in Environmental Science and Technology , vol.35 , Issue.5 , pp. 469-486
    • Vats, P.1    Bhattacharyya, M.S.2    Banerjee, U.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.