메뉴 건너뛰기




Volumn 45, Issue 7, 2010, Pages 1115-1120

Purification and characterization of nitrilase from Fusarium solani IMI196840

Author keywords

Characterization; Fusarium solani; Nitrilase; Nitriles; Purification

Indexed keywords

4-CYANOPYRIDINE; ASPERGILLUS ORYZAE; BENZONITRILES; CHEMOSELECTIVE; CIRCULAR DICHROISM; CULTURE BROTHS; CYANOPYRIDINES; FLUORESCENCE SPECTRA; FUSARIUM SOLANI; GEL FILTRATION; GIBBERELLA ZEAE; HOMO-OLIGOMERS; HYDROLASES; MASS SPECTROMETRY ANALYSIS; MELTING TEMPERATURES; NITRILASE; NITRILES; OPTIMUM CONDITIONS; SDS-PAGE; SECONDARY STRUCTURES; TERTIARY STRUCTURES;

EID: 77954819130     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.03.033     Document Type: Article
Times cited : (30)

References (28)
  • 1
    • 37349104193 scopus 로고    scopus 로고
    • Selection and screening for enzymes of nitrile metabolism
    • Martínková L., Vejvoda V., Křen V. Selection and screening for enzymes of nitrile metabolism. J Biotechnol 2008, 133:318-326.
    • (2008) J Biotechnol , vol.133 , pp. 318-326
    • Martínková, L.1    Vejvoda, V.2    Křen, V.3
  • 2
    • 0041692758 scopus 로고    scopus 로고
    • Synthetic applications of nitrile-converting enzymes
    • Martínková L., Mylerová V. Synthetic applications of nitrile-converting enzymes. Curr Org Chem 2003, 7:1279-1295.
    • (2003) Curr Org Chem , vol.7 , pp. 1279-1295
    • Martínková, L.1    Mylerová, V.2
  • 3
    • 0345167149 scopus 로고    scopus 로고
    • The nitrilase family of CN hydrolysing enzymes - a comparative study
    • O'Reilly C., Turner P.D. The nitrilase family of CN hydrolysing enzymes - a comparative study. J Appl Microbiol 2003, 95:1161-1174.
    • (2003) J Appl Microbiol , vol.95 , pp. 1161-1174
    • O'Reilly, C.1    Turner, P.D.2
  • 4
    • 0037209758 scopus 로고    scopus 로고
    • The nitrile-degrading enzymes: current status and future prospects
    • Banerjee A., Sharma R., Banerjee U.C. The nitrile-degrading enzymes: current status and future prospects. Appl Microbiol Biotechnol 2002, 60:33-44.
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 33-44
    • Banerjee, A.1    Sharma, R.2    Banerjee, U.C.3
  • 6
    • 0000127965 scopus 로고
    • Occurrence, preparation and general properties of the enzyme
    • Thimann K.V., Mahadevan S., Nitrilase I. Occurrence, preparation and general properties of the enzyme. Arch Biochem Biophys 1964, 105:133-141.
    • (1964) Arch Biochem Biophys , vol.105 , pp. 133-141
    • Thimann, K.V.1    Mahadevan, S.2    Nitrilase, I.3
  • 7
    • 0001713878 scopus 로고
    • Ricinine nitrilase II. Purification and properties
    • Hook R.H., Robinson W.G. Ricinine nitrilase II. Purification and properties. J Biol Chem 1964, 239:4263-4267.
    • (1964) J Biol Chem , vol.239 , pp. 4263-4267
    • Hook, R.H.1    Robinson, W.G.2
  • 8
    • 0342803567 scopus 로고    scopus 로고
    • Distribution of aldoxime dehydratase in microorganisms
    • Kato Y., Ooi R., Asano Y. Distribution of aldoxime dehydratase in microorganisms. Appl Environ Microbiol 2000, 66:2290-2296.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2290-2296
    • Kato, Y.1    Ooi, R.2    Asano, Y.3
  • 12
    • 0024788506 scopus 로고
    • Induction, purification, and characterization of the nitrilase of Fusarium oxysporum f. sp. melonis
    • Goldlust A., Bohak Z. Induction, purification, and characterization of the nitrilase of Fusarium oxysporum f. sp. melonis. Biotechnol Appl Biochem 1989, 11:581-601.
    • (1989) Biotechnol Appl Biochem , vol.11 , pp. 581-601
    • Goldlust, A.1    Bohak, Z.2
  • 13
    • 0017668205 scopus 로고
    • Fungal degradation of aromatic nitriles. Enzymology of C-N cleavage by Fusarium solani
    • Harper D.B. Fungal degradation of aromatic nitriles. Enzymology of C-N cleavage by Fusarium solani. Biochem J 1977, 167:685-692.
    • (1977) Biochem J , vol.167 , pp. 685-692
    • Harper, D.B.1
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 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
  • 17
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Böhm G., Muhr R., Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng 1992, 5:191-195.
    • (1992) Protein Eng , vol.5 , pp. 191-195
    • Böhm, G.1    Muhr, R.2    Jaenicke, R.3
  • 18
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N., Woody R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 1993, 209:32-44.
    • (1993) Anal Biochem , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 19
    • 0027190626 scopus 로고
    • An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum
    • Deléage G., Geourjon C. An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput Appl Biosci 1993, 9:197-199.
    • (1993) Comput Appl Biosci , vol.9 , pp. 197-199
    • Deléage, G.1    Geourjon, C.2
  • 20
    • 77954814520 scopus 로고    scopus 로고
    • http://dicroprot-pbil.ibcp.fr/.
  • 22
    • 0033227463 scopus 로고    scopus 로고
    • Characterization of an inducible nitrilase from a thermophilic bacillus
    • Almatawah Q.A., Cramp R., Cowan D.A. Characterization of an inducible nitrilase from a thermophilic bacillus. Extremophiles 1999, 3:283-291.
    • (1999) Extremophiles , vol.3 , pp. 283-291
    • Almatawah, Q.A.1    Cramp, R.2    Cowan, D.A.3
  • 23
    • 0032532430 scopus 로고    scopus 로고
    • Characterization and partial purification of an enantioselective arylacetonitrilase from Pseudomonas fluorescens DSM 7155
    • Layh N., Parratt J., Willetts A. Characterization and partial purification of an enantioselective arylacetonitrilase from Pseudomonas fluorescens DSM 7155. J Mol Catal B: Enzym 1998, 5:467-474.
    • (1998) J Mol Catal B: Enzym , vol.5 , pp. 467-474
    • Layh, N.1    Parratt, J.2    Willetts, A.3
  • 25
    • 27744507286 scopus 로고    scopus 로고
    • Nitrilase from Pseudomonas fluorescens EBC191: cloning and heterologous expression of the genes and biochemical characterization of the recombinant enzyme
    • Kiziak C., Conradt D., Stolz A., Mattes R., Klein J. Nitrilase from Pseudomonas fluorescens EBC191: cloning and heterologous expression of the genes and biochemical characterization of the recombinant enzyme. Microbiology 2005, 151:3639-3648.
    • (2005) Microbiology , vol.151 , pp. 3639-3648
    • Kiziak, C.1    Conradt, D.2    Stolz, A.3    Mattes, R.4    Klein, J.5
  • 26
    • 0025690724 scopus 로고
    • A novel nitrilase, arylacetonitrilase, of Alcaligenes faecalis JM3. Purification and characterization
    • Nagasawa T., Mauger J., Yamada H. A novel nitrilase, arylacetonitrilase, of Alcaligenes faecalis JM3. Purification and characterization. Eur J Biochem 1990, 194:765-772.
    • (1990) Eur J Biochem , vol.194 , pp. 765-772
    • Nagasawa, T.1    Mauger, J.2    Yamada, H.3
  • 27
    • 0026649436 scopus 로고
    • Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue
    • Kobayashi M., Komeda H., Yanaka N., Nagasawa T., Yamada H. Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue. J Biol Chem 1992, 267:20746-20751.
    • (1992) J Biol Chem , vol.267 , pp. 20746-20751
    • Kobayashi, M.1    Komeda, H.2    Yanaka, N.3    Nagasawa, T.4    Yamada, H.5
  • 28
    • 0026628701 scopus 로고
    • Asymmetric hydrolysis of alpha aminonitriles to optically active amino acids by a nitrilase of Rhodococcus rhodochrous PA-34
    • Bhalla T.C., Miura A., Wakamoto A., Ohba Y., Furuhashi K. Asymmetric hydrolysis of alpha aminonitriles to optically active amino acids by a nitrilase of Rhodococcus rhodochrous PA-34. Appl Microbiol Biotechnol 1992, 37:184-190.
    • (1992) Appl Microbiol Biotechnol , vol.37 , pp. 184-190
    • Bhalla, T.C.1    Miura, A.2    Wakamoto, A.3    Ohba, Y.4    Furuhashi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.