메뉴 건너뛰기




Volumn 47, Issue 23, 2013, Pages 13882-13888

Enhanced stability and chemical resistance of a new nanoscale biocatalyst for accelerating CO2 absorption into a carbonate solution

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION PROCESS; CARBONATE SOLUTIONS; COAL COMBUSTION FLUE GAS; COMPOSITE NANOPARTICLES; ENHANCED STABILITY; FLAME SPRAY PYROLYSIS METHODS; INACTIVATION KINETICS; SILICA NANOPARTICLES;

EID: 84889805868     PISSN: 0013936X     EISSN: 15205851     Source Type: Journal    
DOI: 10.1021/es4031744     Document Type: Article
Times cited : (60)

References (35)
  • 7
    • 0010986346 scopus 로고
    • The pH-activity curve of bovine carbonic anhydrase and its relationship to the inhibition of the enzyme by anions
    • Kernohan, J. C. The pH-activity curve of bovine carbonic anhydrase and its relationship to the inhibition of the enzyme by anions Biochim. Biophys. Acta 1965, 96, 304-317
    • (1965) Biochim. Biophys. Acta , vol.96 , pp. 304-317
    • Kernohan, J.C.1
  • 11
    • 1542304635 scopus 로고    scopus 로고
    • Synthetic analogues relevant to the structure and function of zinc enzymes
    • Parkin, G. Synthetic analogues relevant to the structure and function of zinc enzymes Chem. Rev. 2004, 104, 699-767
    • (2004) Chem. Rev. , vol.104 , pp. 699-767
    • Parkin, G.1
  • 12
    • 79953052183 scopus 로고    scopus 로고
    • 2 sequestration using purified carbonic anhydrase from indigenous bacterial strains immobilized on biopolymeric materials
    • 2 sequestration using purified carbonic anhydrase from indigenous bacterial strains immobilized on biopolymeric materials Enzyme Microb. Technol. 2011, 48, 416-426
    • (2011) Enzyme Microb. Technol. , vol.48 , pp. 416-426
    • Sharma, A.1    Bhattacharya, A.2    Shrivastava, A.3
  • 15
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization - Aqueous and non-aqueous environment
    • Iyer, P. V.; Ananthanarayan, L. Enzyme stability and stabilization- Aqueous and non-aqueous environment Process Biochem. 2008, 43, 1019-1032
    • (2008) Process Biochem. , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 19
    • 33751256536 scopus 로고    scopus 로고
    • Nanoscale biocatalyst systems
    • Wang, P. Nanoscale biocatalyst systems Curr. Opin. Biotechnol. 2006, 17, 574-579
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 574-579
    • Wang, P.1
  • 20
    • 48249143984 scopus 로고    scopus 로고
    • Kinetics of amorphous silica dissolution and the paradox of the silica polymorphs
    • Dove, P. M.; Han, N.; Wallace, A. F.; De Yoreo, J. J. Kinetics of amorphous silica dissolution and the paradox of the silica polymorphs Proc. Natl. Acad. Sci., U. S. A. 2008, 105, 9903-9908
    • (2008) Proc. Natl. Acad. Sci., U. S. A. , vol.105 , pp. 9903-9908
    • Dove, P.M.1    Han, N.2    Wallace, A.F.3    De Yoreo, J.J.4
  • 21
    • 0007156734 scopus 로고
    • The mechanism reaction between silicate glass and attacking agents. Part 2. Chemical equilibria at glass-solution interfaces
    • Budd, S. M.; Frackiewicz, J. The mechanism reaction between silicate glass and attacking agents. Part 2. Chemical equilibria at glass-solution interfaces Phys. Chem. Glasses 1961, 2, 115-118
    • (1961) Phys. Chem. Glasses , vol.2 , pp. 115-118
    • Budd, S.M.1    Frackiewicz, J.2
  • 22
    • 0017559946 scopus 로고
    • Chemical durability of glasses: A thermodynamic approach
    • Paul, A. Chemical durability of glasses: A thermodynamic approach J. Mater. Sci. 1977, 2, 2246-2268
    • (1977) J. Mater. Sci. , vol.2 , pp. 2246-2268
    • Paul, A.1
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M.. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 1976, 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0346761424 scopus 로고
    • The manometric determination of the activity of carbonic anhydrase under varied conditions
    • Roughton, F. J.; Booth, V. H. The manometric determination of the activity of carbonic anhydrase under varied conditions Biochem. J. 1946, 40, 309-319
    • (1946) Biochem. J. , vol.40 , pp. 309-319
    • Roughton, F.J.1    Booth, V.H.2
  • 25
    • 0037403364 scopus 로고    scopus 로고
    • Determination of gas-liquid reaction kinetics with a stirred cell reactor
    • Kucka, L.; Richter, J.; Kenig, E. Y.; Górak, A. Determination of gas-liquid reaction kinetics with a stirred cell reactor Sep. Purif. Technol. 2003, 31, 163-175
    • (2003) Sep. Purif. Technol. , vol.31 , pp. 163-175
    • Kucka, L.1    Richter, J.2    Kenig, E.Y.3    Górak, A.4
  • 26
    • 0011388981 scopus 로고
    • The kinetics of the hydration of carbon dioxide at 25
    • Ho, C.; Sturtevant, J. M. The kinetics of the hydration of carbon dioxide at 25 J. Biol. Chem. 1963, 238, 3499-3501
    • (1963) J. Biol. Chem. , vol.238 , pp. 3499-3501
    • Ho, C.1    Sturtevant, J.M.2
  • 27
    • 0018920181 scopus 로고
    • 2 into buffer solutions containing carbonic anhydrase
    • 2 into buffer solutions containing carbonic anhydrase Chem. Eng. Sci. 1980, 35, 549-557
    • (1980) Chem. Eng. Sci. , vol.35 , pp. 549-557
    • Alper, E.1    Deckwer, W.-D.2
  • 28
    • 0023831921 scopus 로고
    • Solubility and diffusivity of acid gases (carbon dioxide, nitrous oxide) in aqueous alkanolamine solutions
    • Versteeg, G. F.; Van Swaalj, W. Solubility and diffusivity of acid gases (carbon dioxide, nitrous oxide) in aqueous alkanolamine solutions J. Chem. Eng. Data 1988, 33, 29-34
    • (1988) J. Chem. Eng. Data , vol.33 , pp. 29-34
    • Versteeg, G.F.1    Van Swaalj, W.2
  • 29
    • 0029657410 scopus 로고    scopus 로고
    • Estimation of gas solubilities in salt solutions at temperatures from 273 to 363 K
    • Weisenberger, S.; Schumpe, A. Estimation of gas solubilities in salt solutions at temperatures from 273 to 363 K AIChE J. 1996, 42, 298-300
    • (1996) AIChE J. , vol.42 , pp. 298-300
    • Weisenberger, S.1    Schumpe, A.2
  • 30
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry, R.; Eyring, H. Conformation changes of proteins J. Phys. Chem. 1954, 58 (2) 110-120
    • (1954) J. Phys. Chem. , vol.58 , Issue.2 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 31
    • 0020814787 scopus 로고
    • On the role of reversible denaturation (unfolding) in the irreversible thermal inactivation of enzymes
    • Zale, S. E.; Klibanov, A. M. On the role of reversible denaturation (unfolding) in the irreversible thermal inactivation of enzymes Biotechnol. Bioeng. 1983, 25, 2221-2230
    • (1983) Biotechnol. Bioeng. , vol.25 , pp. 2221-2230
    • Zale, S.E.1    Klibanov, A.M.2
  • 32
    • 33846370423 scopus 로고    scopus 로고
    • Flame-sprayed superparamagnetic bare and silica-coated maghemite nanoparticles: Synthesis, characterization, and protein adsorption-desorption
    • Li, D.; Teoh, W. Y.; Selomulya, C.; Woodward, R. C.; Amal, R.; Rosche, B. Flame-sprayed superparamagnetic bare and silica-coated maghemite nanoparticles: Synthesis, characterization, and protein adsorption-desorption Chem. Mater. 2006, 18, 6403-6413
    • (2006) Chem. Mater. , vol.18 , pp. 6403-6413
    • Li, D.1    Teoh, W.Y.2    Selomulya, C.3    Woodward, R.C.4    Amal, R.5    Rosche, B.6
  • 33
    • 0001411337 scopus 로고
    • Cobalt(II) as a probe of the structure and function of carbonic-anhydrase
    • Bertini, I.; Luchinat, C. Cobalt(II) as a probe of the structure and function of carbonic-anhydrase Acc. Chem. Res. 1983, 16, 272-279
    • (1983) Acc. Chem. Res. , vol.16 , pp. 272-279
    • Bertini, I.1    Luchinat, C.2
  • 34
    • 0020109738 scopus 로고
    • The interaction of sulfate with carbonic anhydrase
    • Simonsson, I.; Lindskog, S. The interaction of sulfate with carbonic anhydrase Eur. J. Biochem. 1982, 123, 29-36
    • (1982) Eur. J. Biochem. , vol.123 , pp. 29-36
    • Simonsson, I.1    Lindskog, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.