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Volumn 386, Issue 5, 2005, Pages 435-440

An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters

Author keywords

Carotenoids; cDNA library; Fungi; Lipase

Indexed keywords

CARBOXYLESTERASE; COMPLEMENTARY DNA; TRIACYLGLYCEROL LIPASE; XANTHOPHYLL;

EID: 26844520402     PISSN: 14316730     EISSN: 14316730     Source Type: Journal    
DOI: 10.1515/BC.2005.052     Document Type: Article
Times cited : (23)

References (33)
  • 1
    • 0023324420 scopus 로고
    • Effect of Tween 80 and oleic acid on ligninase production by Phanerochaete chrysosporium INA-12
    • Asther, M., Corrieu, G., Drapron, R., and Odier, E. (1987). Effect of Tween 80 and oleic acid on ligninase production by Phanerochaete chrysosporium INA-12. Enzyme Microb. Technol. 9, 245-249.
    • (1987) Enzyme Microb. Technol. , vol.9 , pp. 245-249
    • Asther, M.1    Corrieu, G.2    Drapron, R.3    Odier, E.4
  • 2
    • 0032530679 scopus 로고    scopus 로고
    • Candida rugosa lipases: Molecular biology and versatility in biotechnology
    • Benjamin, S. and Pandey, A. (1998). Candida rugosa lipases: Molecular biology and versatility in biotechnology. Yeast 14, 1069-1087.
    • (1998) Yeast , vol.14 , pp. 1069-1087
    • Benjamin, S.1    Pandey, A.2
  • 3
    • 1842502634 scopus 로고    scopus 로고
    • Aspergillus niger protein EstA defines a new class of fungal esterases within the α/β hydrolase fold superfamily of proteins
    • Bourne, Y., Hasper, A., Chahinian, H., Juin, M., de Graaff, L., and Marchot, P. (2004). Aspergillus niger protein EstA defines a new class of fungal esterases within the α/β hydrolase fold superfamily of proteins. Structure 12, 677-687.
    • (2004) Structure , vol.12 , pp. 677-687
    • Bourne, Y.1    Hasper, A.2    Chahinian, H.3    Juin, M.4    de Graaff, L.5    Marchot, P.6
  • 4
    • 0001887728 scopus 로고    scopus 로고
    • Determination of free and bound carotenoids in paprika (Capsicum annuum L.) by LC/MS
    • Breithaupt, D.E. and Schwack, W. (2000). Determination of free and bound carotenoids in paprika (Capsicum annuum L.) by LC/MS. Eur. Food Res. Technol. 211, 52-55.
    • (2000) Eur. Food Res. Technol. , vol.211 , pp. 52-55
    • Breithaupt, D.E.1    Schwack, W.2
  • 5
    • 0036006609 scopus 로고    scopus 로고
    • Differentiation between lutein monoester regioisomers and detection of lutein diesters from marigold flowers (Tagetes erecta L.) and several fruits by liquid chromatography-mass spectrometry
    • Breithaupt, D.E., Wirt, U., and Bamedi, A. (2002). Differentiation between lutein monoester regioisomers and detection of lutein diesters from marigold flowers (Tagetes erecta L.) and several fruits by liquid chromatography-mass spectrometry. J. Agric. Food Chem. 50, 66-70.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 66-70
    • Breithaupt, D.E.1    Wirt, U.2    Bamedi, A.3
  • 7
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins
    • Cygler, M., Schrag, J.D., Sussman, J.L., Harel, M., Silman, I., Gentry, M.K., and Doctor, B.P. (1993). Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci. 2, 366-382.
    • (1993) Protein Sci. , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 9
    • 0029644244 scopus 로고
    • Structure uncomplexed and linoleatebound Candida cylindracea cholesterol esterase
    • Ghosh, D., Wawrzak, Z., Pletnev, V.Z., Li, N., Kaiser, R., Pangborn, W., et al. (1995). Structure uncomplexed and linoleatebound Candida cylindracea cholesterol esterase. Structure 3, 279-288.
    • (1995) Structure , vol.3 , pp. 279-288
    • Ghosh, D.1    Wawrzak, Z.2    Pletnev, V.Z.3    Li, N.4    Kaiser, R.5    Pangborn, W.6
  • 10
    • 85069033784 scopus 로고    scopus 로고
    • Gish, W. (2004). http://blast.wustl.edu.
    • (2004)
    • Gish, W.1
  • 11
    • 0028103723 scopus 로고
    • Two conformational states of Candida rugosa lipase
    • Grochulski, P., Li, Y., Schrag, J.D., and Cygler, M. (1994). Two conformational states of Candida rugosa lipase. Protein Sci. 3, 82-91.
    • (1994) Protein Sci. , vol.3 , pp. 82-91
    • Grochulski, P.1    Li, Y.2    Schrag, J.D.3    Cygler, M.4
  • 12
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N. and Peitsch, M.C. (1997). SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 14
    • 0028337084 scopus 로고
    • Localization of lipolytic and esterolytic activities in Tyromyces sambuceus, a 4-decanolide-producing basidiomycete
    • Hädrich-Meyer, S. and Berger, R.G. (1994). Localization of lipolytic and esterolytic activities in Tyromyces sambuceus, a 4-decanolide-producing basidiomycete. Appl. Microbiol. Biotechnol. 41, 210-214.
    • (1994) Appl. Microbiol. Biotechnol. , vol.41 , pp. 210-214
    • Hädrich-Meyer, S.1    Berger, R.G.2
  • 15
    • 0026843925 scopus 로고
    • Chemical and physiological behaviour of feed carotenoids and their effects on pigmentation
    • Hencken, H. (1992). Chemical and physiological behaviour of feed carotenoids and their effects on pigmentation. Poult. Sci. 71, 711-717.
    • (1992) Poult. Sci. , vol.71 , pp. 711-717
    • Hencken, H.1
  • 16
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins, D., Thompson, J., Gibson, T., Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 17
    • 12644295852 scopus 로고
    • Lipid metabolism of mushroom mycelia
    • Holtz, R.B. and Smith, D.E. (1978). Lipid metabolism of mushroom mycelia. Mushroom Sci. 10, 437-444.
    • (1978) Mushroom Sci. , vol.10 , pp. 437-444
    • Holtz, R.B.1    Smith, D.E.2
  • 18
    • 0027979972 scopus 로고
    • Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea
    • Kaiser, R., Erman, M., Duax, W.L., Ghosh, D., and Jörnvall, H. (1994) Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea. FEBS Lett. 337, 123-127.
    • (1994) FEBS Lett. , vol.337 , pp. 123-127
    • Kaiser, R.1    Erman, M.2    Duax, W.L.3    Ghosh, D.4    Jörnvall, H.5
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1979). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1979) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0034775358 scopus 로고    scopus 로고
    • Lutein, zeaxanthin, and the macular pigment
    • Landrum, J.T. and Bone, R.A. (2001). Lutein, zeaxanthin, and the macular pigment. Arch. Biochem. Biophys. 385, 28-40.
    • (2001) Arch. Biochem. Biophys. , vol.385 , pp. 28-40
    • Landrum, J.T.1    Bone, R.A.2
  • 21
    • 0024097963 scopus 로고
    • Structure of human serum cholinesterase
    • Lockridge, O. (1988). Structure of human serum cholinesterase. Bioessays 9, 125-128.
    • (1988) Bioessays , vol.9 , pp. 125-128
    • Lockridge, O.1
  • 22
    • 0042386531 scopus 로고    scopus 로고
    • Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: Crystal structure of the lipase 2 isoenzyme at 1.97 Å resolution
    • Mancheno, J.M., Pernas, M.A., Martinez, M.J., Ochoa, B., Rua, M.L., and Hermoso, J.A. (2003). Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97 Å resolution. J. Mol. Biol. 332, 1059-1069.
    • (2003) J. Mol. Biol. , vol.332 , pp. 1059-1069
    • Mancheno, J.M.1    Pernas, M.A.2    Martinez, M.J.3    Ochoa, B.4    Rua, M.L.5    Hermoso, J.A.6
  • 24
    • 0027944215 scopus 로고
    • Detection of lipase activity on ultrathin-layer isoelectric focusing gels
    • Nuero, O.M., Garcia-Lepe, R., Lahoz, C., Santamaria, F., and Reyes, F. (1994). Detection of lipase activity on ultrathin-layer isoelectric focusing gels. Anal. Biochem. 222, 503-505.
    • (1994) Anal. Biochem. , vol.222 , pp. 503-505
    • Nuero, O.M.1    Garcia-Lepe, R.2    Lahoz, C.3    Santamaria, F.4    Reyes, F.5
  • 27
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R. and Lipman, D.J. (1988). Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85, 2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 28
    • 0031857235 scopus 로고    scopus 로고
    • Biodegradative and biosynthetic capacities of mushrooms: Present and future strategies
    • Rajarathnam, S., Shashirekha, M.N., and Bano, Z. (1998). Biodegradative and biosynthetic capacities of mushrooms: present and future strategies. Crit. Rev. Biotechnol. 18, 91-236.
    • (1998) Crit. Rev. Biotechnol. , vol.18 , pp. 91-236
    • Rajarathnam, S.1    Shashirekha, M.N.2    Bano, Z.3
  • 30
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M.C. (2003). SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 31
    • 0025332109 scopus 로고
    • Separation and characterization of two molecular forms of Geotrichum candidum lipase
    • Sugihara, A., Shimada, Y., and Tominaga, Y. (1990) Separation and characterization of two molecular forms of Geotrichum candidum lipase. J. Biochem. 107, 426-430.
    • (1990) J. Biochem. , vol.107 , pp. 426-430
    • Sugihara, A.1    Shimada, Y.2    Tominaga, Y.3
  • 32
    • 0027467140 scopus 로고
    • Bile salt-activated lipase. A multiple function lipolytic enzyme
    • Wang, C.-S. and Hartsuck, J.A. (1993). Bile salt-activated lipase. A multiple function lipolytic enzyme. Biochim. Biophys. Acta 1166, 1-19.
    • (1993) Biochim. Biophys. Acta , vol.1166 , pp. 1-19
    • Wang, C.-S.1    Hartsuck, J.A.2
  • 33
    • 0037426291 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of carotenoid esters of marigold flowers (Tagetes erecta L.) and red paprika (Capsicum annuum L.) by commercial lipases and Pleurotus sapidus extracellular lipase
    • Zorn, H., Breithaupt, D.E., Takenberg, M., Schwack,W., and Berger, R.G. (2003). Enzymatic hydrolysis of carotenoid esters of marigold flowers (Tagetes erecta L.) and red paprika (Capsicum annuum L.) by commercial lipases and Pleurotus sapidus extracellular lipase. Enzyme Microb. Technol. 32, 623-628.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 623-628
    • Zorn, H.1    Breithaupt, D.E.2    Takenberg, M.3    Schwack, W.4    Berger, R.G.5


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