메뉴 건너뛰기




Volumn 221, Issue 1-3, 2008, Pages 543-551

Peptides removing in enzymatic membrane bioreactor

Author keywords

Catalytic membrane; Dynamic membrane; Enzyme adsorption; Membrane reactor; Peptide hydrolysis

Indexed keywords

CATALYSIS; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; HYDROLYSIS; PEPTIDES; POLYPEPTIDES;

EID: 38349029092     PISSN: 00119164     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.desal.2007.01.115     Document Type: Article
Times cited : (13)

References (26)
  • 1
    • 2342534954 scopus 로고    scopus 로고
    • Fermentation of individual proteins for protease production by Serratia marcescens
    • Ustariz F.J., Laca A., Garcia L.A., and Diaz M. Fermentation of individual proteins for protease production by Serratia marcescens. Biochem. Eng. J. 19 (2004) 147-153
    • (2004) Biochem. Eng. J. , vol.19 , pp. 147-153
    • Ustariz, F.J.1    Laca, A.2    Garcia, L.A.3    Diaz, M.4
  • 2
    • 0029948243 scopus 로고    scopus 로고
    • Thermostable alkaline proteases of Bacillus licheniformis MIR 29: isolation, production and characterization
    • Ferrero M.A., Castro G.R., Abate C.M., Baigori M.D., and Sineriz F. Thermostable alkaline proteases of Bacillus licheniformis MIR 29: isolation, production and characterization. Appl. Microbiol. Biotechnol. 45 (1996) 327-332
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 327-332
    • Ferrero, M.A.1    Castro, G.R.2    Abate, C.M.3    Baigori, M.D.4    Sineriz, F.5
  • 3
    • 0033180054 scopus 로고    scopus 로고
    • Production and characterization of metalloproteases synthesized concomitantly with δ-endotoxin by Bacillus thuringiensis subsp. kurstaki strain grown on gruel-based media
    • Zouari N., and Jaoua S. Production and characterization of metalloproteases synthesized concomitantly with δ-endotoxin by Bacillus thuringiensis subsp. kurstaki strain grown on gruel-based media. Enzyme Microbial. Technol. 25 (1999) 364-371
    • (1999) Enzyme Microbial. Technol. , vol.25 , pp. 364-371
    • Zouari, N.1    Jaoua, S.2
  • 4
    • 21044432132 scopus 로고    scopus 로고
    • Immobilization of β-glucosidase on carbon nanotubes
    • Gomez J.M., Romero M.D., and Fernandez T.M. Immobilization of β-glucosidase on carbon nanotubes. Catal. Lett. 101 3-4 (2005) 275-278
    • (2005) Catal. Lett. , vol.101 , Issue.3-4 , pp. 275-278
    • Gomez, J.M.1    Romero, M.D.2    Fernandez, T.M.3
  • 5
    • 0000450509 scopus 로고    scopus 로고
    • Plant seed oil-bodies as an immobilization matrix for a recombinant xylanase from the rumen fungus Neocallimastix patriciarum
    • Liu J.-H., et al. Plant seed oil-bodies as an immobilization matrix for a recombinant xylanase from the rumen fungus Neocallimastix patriciarum. Mol. Breed. 3 6 (1997) 463-470
    • (1997) Mol. Breed. , vol.3 , Issue.6 , pp. 463-470
    • Liu, J.-H.1
  • 6
    • 0007679927 scopus 로고    scopus 로고
    • Titanosilicates as supports for an enzymatic alcoholysis reaction
    • Serralha F.N., et al. Titanosilicates as supports for an enzymatic alcoholysis reaction. Reaction Kinet. Catal. Lett. 69 2 (2000) 217-222
    • (2000) Reaction Kinet. Catal. Lett. , vol.69 , Issue.2 , pp. 217-222
    • Serralha, F.N.1
  • 7
    • 0030617257 scopus 로고    scopus 로고
    • Hydrolysis and regioselective tranesterification catalyzed by immobilized lipases in membrane bioreactors
    • Giorno L., Molinari R., Natoli M., and Drioli E. Hydrolysis and regioselective tranesterification catalyzed by immobilized lipases in membrane bioreactors. J. Membr. Sci. 125 (1997) 177-187
    • (1997) J. Membr. Sci. , vol.125 , pp. 177-187
    • Giorno, L.1    Molinari, R.2    Natoli, M.3    Drioli, E.4
  • 8
    • 0030617256 scopus 로고    scopus 로고
    • A multiphase/extractive enzyme membrane reactor for production of diltiazem chiral intermediate
    • Lopez J.L., and Matson S.L. A multiphase/extractive enzyme membrane reactor for production of diltiazem chiral intermediate. J. Membr. Sci. 125 (1997) 189-211
    • (1997) J. Membr. Sci. , vol.125 , pp. 189-211
    • Lopez, J.L.1    Matson, S.L.2
  • 10
    • 1542639603 scopus 로고    scopus 로고
    • Catalytic membrane reactors
    • Drioli E., and Giorno L. Catalytic membrane reactors. Chem. Ind. 1 (1996) 19-22
    • (1996) Chem. Ind. , vol.1 , pp. 19-22
    • Drioli, E.1    Giorno, L.2
  • 11
    • 1242286856 scopus 로고    scopus 로고
    • Membrane reactors
    • Trusek-Hołownia A. (Ed), Argi, Wroclaw
    • Noworyta A. Membrane reactors. In: Trusek-Hołownia A. (Ed). Membrane Separations (2001), Argi, Wroclaw 97-119
    • (2001) Membrane Separations , pp. 97-119
    • Noworyta, A.1
  • 12
    • 33747800077 scopus 로고    scopus 로고
    • Immobilization of lipase from Candida rugosa on electrospun polysulfone nanofibrous membranes by adsorption
    • Wang Z.-G., Wang J.-O., and Xu Z.-K. Immobilization of lipase from Candida rugosa on electrospun polysulfone nanofibrous membranes by adsorption. J. Mol. Catal. B. Enz. 42 1-2 (2006) 45-51
    • (2006) J. Mol. Catal. B. Enz. , vol.42 , Issue.1-2 , pp. 45-51
    • Wang, Z.-G.1    Wang, J.-O.2    Xu, Z.-K.3
  • 13
    • 0141922885 scopus 로고    scopus 로고
    • Esterase activity of biocomposites constituted by lipases adsorbed on layered zirconium phosphate and phosphonates: selective adsorption of different enzyme isoforms
    • Bellezza F., Cipiciani A., and Costantino U. Esterase activity of biocomposites constituted by lipases adsorbed on layered zirconium phosphate and phosphonates: selective adsorption of different enzyme isoforms. J. Mol. Catal. B. Enz. 26 1-2 (2003) 47-56
    • (2003) J. Mol. Catal. B. Enz. , vol.26 , Issue.1-2 , pp. 47-56
    • Bellezza, F.1    Cipiciani, A.2    Costantino, U.3
  • 14
    • 0000731735 scopus 로고    scopus 로고
    • A. Kondo and T. Urabe, Temperature dependence of activity and conformational changes in a-amylases with different thermostability upon adsorption on ultrafine silica particles, 174 (1) (1995) 191-198.
  • 15
    • 0345764902 scopus 로고    scopus 로고
    • Immobilization of cyclodextringlycosyltransferase (CGTase) from Bacillus firmus in commercial chitosan
    • Sobral K.C.A., et al. Immobilization of cyclodextringlycosyltransferase (CGTase) from Bacillus firmus in commercial chitosan. J. Incl. Phen. Macroc. Chem. 44 1-4 (2002) 383-386
    • (2002) J. Incl. Phen. Macroc. Chem. , vol.44 , Issue.1-4 , pp. 383-386
    • Sobral, K.C.A.1
  • 16
    • 0033914091 scopus 로고    scopus 로고
    • Covalent immobilization of penicillin acylase from Streptomyces lavendulae
    • Torres-Bacete J., et al. Covalent immobilization of penicillin acylase from Streptomyces lavendulae. Biotechnol. Lett. 22 12 (2000) 1011-1014
    • (2000) Biotechnol. Lett. , vol.22 , Issue.12 , pp. 1011-1014
    • Torres-Bacete, J.1
  • 17
    • 0346059510 scopus 로고    scopus 로고
    • Covalent immobilization of invertase on microporous pHEMA-GMA membrane
    • Danisman T., Tan S., Kacar Y., and Ergene A. Covalent immobilization of invertase on microporous pHEMA-GMA membrane. Food Chem. 85 3 (2004) 461-466
    • (2004) Food Chem. , vol.85 , Issue.3 , pp. 461-466
    • Danisman, T.1    Tan, S.2    Kacar, Y.3    Ergene, A.4
  • 18
    • 0032306235 scopus 로고    scopus 로고
    • Sol-gel immobilized glucose-oxidase: calorimetric investigations of enzyme activities
    • Georgi U., Graebner H., Roewer G., and Wolf G. Sol-gel immobilized glucose-oxidase: calorimetric investigations of enzyme activities. J. Sol-Gel Sci. Technol. 13 1-3 (1998) 295-298
    • (1998) J. Sol-Gel Sci. Technol. , vol.13 , Issue.1-3 , pp. 295-298
    • Georgi, U.1    Graebner, H.2    Roewer, G.3    Wolf, G.4
  • 19
    • 11144258917 scopus 로고    scopus 로고
    • Activity of glucose oxidase entrapped in mesoporous gels
    • Han K., et al. Activity of glucose oxidase entrapped in mesoporous gels. Biochem. Eng. J. 22 2 (2005) 161-166
    • (2005) Biochem. Eng. J. , vol.22 , Issue.2 , pp. 161-166
    • Han, K.1
  • 20
    • 0029626674 scopus 로고
    • Hyperstabilization of a thermophilic esterase by multipoint covalent attachment
    • Fernandez-Lafuente R., Cowan D.A., and Wood A.N.P. Hyperstabilization of a thermophilic esterase by multipoint covalent attachment. Enzyme Microb. Technol. 17 4 (1995) 366-372
    • (1995) Enzyme Microb. Technol. , vol.17 , Issue.4 , pp. 366-372
    • Fernandez-Lafuente, R.1    Cowan, D.A.2    Wood, A.N.P.3
  • 21
    • 0037056572 scopus 로고    scopus 로고
    • Catalytic membrane preparation for enzymatic hydrolysis reactions carried out in the membrane phase contactor
    • Trusek-Holownia A., and Noworyta A. Catalytic membrane preparation for enzymatic hydrolysis reactions carried out in the membrane phase contactor. Desalination 144 (2002) 427-432
    • (2002) Desalination , vol.144 , pp. 427-432
    • Trusek-Holownia, A.1    Noworyta, A.2
  • 23
    • 0015072056 scopus 로고
    • Fluorescence reaction for amino acids
    • Roth M. Fluorescence reaction for amino acids. Anal. Chem. 43 (1971) 880-882
    • (1971) Anal. Chem. , vol.43 , pp. 880-882
    • Roth, M.1
  • 24
    • 0030569734 scopus 로고    scopus 로고
    • A rapid method for determining kinetic parameters of enzymes exhibiting nonlinear thermal inactivation behavior
    • Nath S. A rapid method for determining kinetic parameters of enzymes exhibiting nonlinear thermal inactivation behavior. Biotechnol. Bioeng. 49 (1996) 106-110
    • (1996) Biotechnol. Bioeng. , vol.49 , pp. 106-110
    • Nath, S.1
  • 25
    • 0004155427 scopus 로고
    • W.H. Freeman and Company, New York
    • Stryer L. Biochemistry (1995), W.H. Freeman and Company, New York
    • (1995) Biochemistry
    • Stryer, L.1
  • 26
    • 21844465103 scopus 로고    scopus 로고
    • A catalytic membrane for hydrolysis reaction carried out in the two-liquid phase system - membrane preparation and characterization, mathematical model of the process
    • Trusek-Holownia A. A catalytic membrane for hydrolysis reaction carried out in the two-liquid phase system - membrane preparation and characterization, mathematical model of the process. J. Membr. Sci. 259 (2005) 74-84
    • (2005) J. Membr. Sci. , vol.259 , pp. 74-84
    • Trusek-Holownia, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.