메뉴 건너뛰기




Volumn 6, Issue 1, 2007, Pages 31-35

Irreversible affinity immobilization of lentil seedling amine oxidase with activity retention

Author keywords

Activity; Affinity; Amine oxidase; Immobilization

Indexed keywords


EID: 84907103041     PISSN: 15829596     EISSN: 18433707     Source Type: Journal    
DOI: 10.30638/eemj.2007.006     Document Type: Article
Times cited : (3)

References (20)
  • 1
    • 0346780250 scopus 로고    scopus 로고
    • Directed Evolution of Enzymes: New Biocatalysts for Asymmetric Synthesis
    • Alexeeva M., Carr R., Turner N. J., (2003), Directed Evolution of Enzymes: New Biocatalysts for Asymmetric Synthesis, Org. Biomol. Chem., 1, 4133-4137.
    • (2003) Org. Biomol. Chem , vol.1 , pp. 4133-4137
    • Alexeeva, M.1    Carr, R.2    Turner, N.J.3
  • 3
    • 0031702661 scopus 로고    scopus 로고
    • Serum amine oxidase can specifically recognize and oxidize aminohexyl (AH) chains on AH-sepharose support: Single-step affinity immobilization
    • Befani O., Graziani M.T., Agostinelli E., Grippa E., Mondoví B., Mateescu M.-A., (1998), Serum amine oxidase can specifically recognize and oxidize aminohexyl (AH) chains on AH-sepharose support: single-step affinity immobilization, Biotechnol. Appl. Biochem., 28, 99-104.
    • (1998) Biotechnol. Appl. Biochem , vol.28 , pp. 99-104
    • Befani, O.1    Graziani, M.T.2    Agostinelli, E.3    Grippa, E.4    Mondoví, B.5    Mateescu, M.-A.6
  • 4
    • 0031013630 scopus 로고    scopus 로고
    • Amperometric biosensors for diamine using diamine oxidase purified from porcine kidney
    • Bouvrette P., Male K.B., Luong J.H.T., Gibbs B.F., (1997), Amperometric biosensors for diamine using diamine oxidase purified from porcine kidney, Enzyme Microb. Technol., 20, 32-38.
    • (1997) Enzyme Microb. Technol , vol.20 , pp. 32-38
    • Bouvrette, P.1    Male, K.B.2    Luong, J.H.T.3    Gibbs, B.F.4
  • 5
    • 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., (1976), A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0034992341 scopus 로고    scopus 로고
    • Immobilization of native and poly(Ethylene glycol)-treated (‘PEGylated’) bovine serum amine oxidase into a biocompatible hydrogel
    • Demers N., Agostinelli E., Averill-Bates D.A., Fortier G., (2001), Immobilization of native and poly(ethylene glycol)-treated (‘PEGylated’) bovine serum amine oxidase into a biocompatible hydrogel, Biotechnol. Appl. Biochem., 33, 201-207.
    • (2001) Biotechnol. Appl. Biochem , vol.33 , pp. 201-207
    • Demers, N.1    Agostinelli, E.2    Averill-Bates, D.A.3    Fortier, G.4
  • 8
    • 0000369961 scopus 로고
    • Diamine oxidase from Lens esculenta seedlings: Purification and properties
    • Floris G., Giartosio A., Rinaldi A., (1983), Diamine oxidase from Lens esculenta seedlings: purification and properties, Phytochemistry, 22, 1871-1874.
    • (1983) Phytochemistry , vol.22 , pp. 1871-1874
    • Floris, G.1    Giartosio, A.2    Rinaldi, A.3
  • 9
    • 0000977882 scopus 로고
    • Isolation and characterisation of Populus isoperoxidases involved in the last step of lignin formation
    • Imberty A., Goldberg R., Catesson A.M., (1985), Isolation and characterisation of Populus isoperoxidases involved in the last step of lignin formation, Planta, 164, 221-226.
    • (1985) Planta , vol.164 , pp. 221-226
    • Imberty, A.1    Goldberg, R.2    Catesson, A.M.3
  • 11
    • 0019366638 scopus 로고
    • Quantitation and estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate
    • Leonowicz A., Grzywnowicz K., (1981), Quantitation and estimation of laccase forms in some white-rot fungi using syringaldazine as a substrate, Enzyme Microb. Technol., 3, 55-58.
    • (1981) Enzyme Microb. Technol , vol.3 , pp. 55-58
    • Leonowicz, A.1    Grzywnowicz, K.2
  • 16
    • 0034034017 scopus 로고    scopus 로고
    • Redox hydrogel-based amperometric bioenzyme electrodes for fish freshness monitoring
    • Niculescu M., Nistor C., Frebort I., Pec P., Mattiasson B., Csöregi E., (2000), Redox hydrogel-based amperometric bioenzyme electrodes for fish freshness monitoring, Anal. Chem., 72, 1591-1597.
    • (2000) Anal. Chem , vol.72 , pp. 1591-1597
    • Niculescu, M.1    Nistor, C.2    Frebort, I.3    Pec, P.4    Mattiasson, B.5    Csöregi, E.6
  • 17
    • 0034194346 scopus 로고    scopus 로고
    • Development of the enzyme reactor system with an amperometric detection and application to estimation of the incipient stage of spoilage of chicken
    • Okumaa H., Okazaki W., Usamib R., Horikoshi K., (2000), Development of the enzyme reactor system with an amperometric detection and application to estimation of the incipient stage of spoilage of chicken, Anal. Chim. Acta, 411, 37-43.
    • (2000) Anal. Chim. Acta , vol.411 , pp. 37-43
    • Okumaa, H.1    Okazaki, W.2    Usamib, R.3    Horikoshi, K.4
  • 18
    • 10944269266 scopus 로고    scopus 로고
    • Role of phenolics in the antioxidative status of the resurrection plant Ramonda serbica during dehydration and rehydration
    • Sgherri C., Stevanovic B., Navari-Izzo F., (2004), Role of phenolics in the antioxidative status of the resurrection plant Ramonda serbica during dehydration and rehydration, Physiol. Plant., 122, 478-485.
    • (2004) Physiol. Plant , vol.122 , pp. 478-485
    • Sgherri, C.1    Stevanovic, B.2    Navari-Izzo, F.3
  • 20
    • 29044440810 scopus 로고    scopus 로고
    • Applications of oxidoreductases: Recent progress
    • Xu F., (2005), Applications of oxidoreductases: Recent progress, Ind. Biotechnol., 1, 38-50.
    • (2005) Ind. Biotechnol , vol.1 , pp. 38-50
    • Xu, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.