메뉴 건너뛰기




Volumn 29, Issue 8, 2007, Pages 1227-1232

Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5

Author keywords

Cutinase; Fusarium venenatum; Recombinant protein

Indexed keywords

CODING SEQUENCE; CUTINASE; FUSARIUM VENENATUM; GLUCOAMYLASE PROMOTER; RECOMBINANT PROTEIN;

EID: 34447124589     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-007-9369-7     Document Type: Article
Times cited : (5)

References (18)
  • 1
    • 0032766404 scopus 로고    scopus 로고
    • Purification, characterization, and heterologous expression in Fusarium venenatum of a novel serine carboxypeptidase from Aspergillus oryzae
    • Blinkovsky AM, Byun T, Brown KM, Golightly EJ (1999) Purification, characterization, and heterologous expression in Fusarium venenatum of a novel serine carboxypeptidase from Aspergillus oryzae. Appl Environ Microbiol 65:3298-3303
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3298-3303
    • Blinkovsky, A.M.1    Byun, T.2    Brown, K.M.3    Golightly, E.J.4
  • 2
    • 0035862423 scopus 로고    scopus 로고
    • Combined use of growth rate correlated and growth rate independent promoters for recombinant glucoamylase production in Fusarium venenatum
    • Gordon C, Thomas S, Griffen A, Robson GD, Trinci APJ, Wiebe MG (2001) Combined use of growth rate correlated and growth rate independent promoters for recombinant glucoamylase production in Fusarium venenatum. FEMS Microbiol Lett 194:229-234
    • (2001) FEMS Microbiol Lett , vol.194 , pp. 229-234
    • Gordon, C.1    Thomas, S.2    Griffen, A.3    Robson, G.D.4    Trinci, A.P.J.5    Wiebe, M.G.6
  • 4
    • 0017863125 scopus 로고
    • Induction of a biopolyester hydrolase (cutinase) by low levels of cutin monomers in Fusarium solani f. sp. pisi
    • Lin TS, Kolattukudy PE (1978) Induction of a biopolyester hydrolase (cutinase) by low levels of cutin monomers in Fusarium solani f. sp. pisi. J Bacteriol 133:942-951
    • (1978) J Bacteriol , vol.133 , pp. 942-951
    • Lin, T.S.1    Kolattukudy, P.E.2
  • 6
    • 0030267827 scopus 로고    scopus 로고
    • Lipase production by lactic acid bacteria and activity on butter oil
    • Meyers SA, Cuppett SL, Hutkins RW (1996) Lipase production by lactic acid bacteria and activity on butter oil. Food Microbiol 13:383-389
    • (1996) Food Microbiol , vol.13 , pp. 383-389
    • Meyers, S.A.1    Cuppett, S.L.2    Hutkins, R.W.3
  • 7
    • 0035907145 scopus 로고    scopus 로고
    • Engineering the pH-optimum of a triglyceride lipase: From predictions based on electrostatic computations to experimental results
    • Neves-Petersen MT, Petersen EI, Fojan P, Noronha M, Madsen RG, Petersen SB (2001) Engineering the pH-optimum of a triglyceride lipase: from predictions based on electrostatic computations to experimental results. J Biotechnol 87:225-254
    • (2001) J Biotechnol , vol.87 , pp. 225-254
    • Neves-Petersen, M.T.1    Petersen, E.I.2    Fojan, P.3    Noronha, M.4    Madsen, R.G.5    Petersen, S.B.6
  • 8
    • 0033045182 scopus 로고    scopus 로고
    • Preparation, isolation, and characterization of cutin monomers and oligomers from tomato peels
    • Osman SF, Irwin P, Fett WF, O'Connor JV, Parris N (1999) Preparation, isolation, and characterization of cutin monomers and oligomers from tomato peels. J Agric Food Chem 47:799-802
    • (1999) J Agric Food Chem , vol.47 , pp. 799-802
    • Osman, S.F.1    Irwin, P.2    Fett, W.F.3    O'Connor, J.V.4    Parris, N.5
  • 9
    • 0027016529 scopus 로고
    • Transformation of filamentous fungi based on hygromycin B and phleomycin resistance markers
    • Punt PJ, van den Hondel CAMJJ (1992) Transformation of filamentous fungi based on hygromycin B and phleomycin resistance markers. Methods Enzymol 216:447-457
    • (1992) Methods Enzymol , vol.216 , pp. 447-457
    • Punt, P.J.1    Den Hondel Camjj, V.2
  • 10
    • 0016682066 scopus 로고
    • Hydrolysis of plant cutin by plant pathogens. Purification, amino acids composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi
    • Purdy RE, Kolattukudy PE (1975) Hydrolysis of plant cutin by plant pathogens. Purification, amino acids composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry 14:2824-2831
    • (1975) Biochemistry , vol.14 , pp. 2824-2831
    • Purdy, R.E.1    Kolattukudy, P.E.2
  • 12
    • 0023119887 scopus 로고
    • Discovery of a cutinase-producing Pseudomonas sp. cohabiting with an apparently nitrogen-fixing Corynebacterium sp. in phyllosphere
    • Sebastian J, Chandra AK, Kolattukudy PE (1987) Discovery of a cutinase-producing Pseudomonas sp. cohabiting with an apparently nitrogen-fixing Corynebacterium sp. in phyllosphere. J Bacteriol 169:131-136
    • (1987) J Bacteriol , vol.169 , pp. 131-136
    • Sebastian, J.1    Chandra, A.K.2    Kolattukudy, P.E.3
  • 13
    • 0029056506 scopus 로고
    • Construction and heterologous expression of a synthetic copy of the cutinase cDNA from Fusarium solani pisi
    • van Gemeren IA, Musters W, van den Hondel CAMJJ, Verrips CT (1995) Construction and heterologous expression of a synthetic copy of the cutinase cDNA from Fusarium solani pisi. J Biotechnol 40:155-162
    • (1995) J Biotechnol , vol.40 , pp. 155-162
    • Van Gemeren, I.A.1    Musters, W.2    Den Hondel Camjj, V.3    Verrips, C.T.4
  • 14
    • 0342699643 scopus 로고    scopus 로고
    • From gene to product in yeast: Production of fungal cutinase
    • Verrips T, Duboc P, Visser C, Sagt C (2000) From gene to product in yeast: production of fungal cutinase. Enzyme Microb Technol 26:812-818
    • (2000) Enzyme Microb Technol , vol.26 , pp. 812-818
    • Verrips, T.1    Duboc, P.2    Visser, C.3    Sagt, C.4
  • 15
    • 0001963676 scopus 로고
    • A convenient growth medium for Neurospora (Medium N)
    • Vogel HJ (1956) A convenient growth medium for Neurospora (Medium N). Microbial Genet Bull 243:112-119
    • (1956) Microbial Genet Bull , vol.243 , pp. 112-119
    • Vogel, H.J.1
  • 16
    • 0036348909 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression of a redox-responsive cutinase from Monilinia fructicola (Wint) honey
    • Wang GY, Michailides TJ, Hammock BD, Lee Y-M, Bostock RM (2002) Molecular cloning, characterization, and expression of a redox-responsive cutinase from Monilinia fructicola (Wint) honey. Fungal Genet Biol 35:261-276
    • (2002) Fungal Genet Biol , vol.35 , pp. 261-276
    • Wang, G.Y.1    Michailides, T.J.2    Hammock, B.D.3    Lee, Y.-M.4    Bostock, R.M.5
  • 17
    • 0034607634 scopus 로고    scopus 로고
    • Growth rate independent production of recombinant glucoamylase by Fusarium venenatum JeRS 325
    • Wiebe MG, Robson GD, Shuster JR, Trinci APJ (2000) Growth rate independent production of recombinant glucoamylase by Fusarium venenatum JeRS 325. Biotechnol Bioeng 68:245-251
    • (2000) Biotechnol Bioeng , vol.68 , pp. 245-251
    • Wiebe, M.G.1    Robson, G.D.2    Shuster, J.R.3    Trinci, A.P.J.4
  • 18
    • 0035917932 scopus 로고    scopus 로고
    • Evolution of a recombinant (glucoamylase-prodcuing) strain of Fusarium venenatum A3/5 in chemostat culture
    • Wiebe MG, Robson GD, Shuster J, Trinci APJ (2001) Evolution of a recombinant (glucoamylase-prodcuing) strain of Fusarium venenatum A3/5 in chemostat culture. Biotechnol Bioeng 73:146-156
    • (2001) Biotechnol Bioeng , vol.73 , pp. 146-156
    • Wiebe, M.G.1    Robson, G.D.2    Shuster, J.3    Trinci, A.P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.