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Volumn 71, Issue 2, 2015, Pages 1199-1206

The Surfactant-Induced Conformational and Activity Alterations in Rhizopus niveus Lipase

Author keywords

ANS; Fluorescence intensity; Mean residual ellipticity; Rhizopus niveus lipase

Indexed keywords

SURFACTANT; TRIACYLGLYCEROL LIPASE;

EID: 84925506484     PISSN: 10859195     EISSN: 15590283     Source Type: Journal    
DOI: 10.1007/s12013-014-0329-2     Document Type: Article
Times cited : (99)

References (29)
  • 1
    • 85047685160 scopus 로고    scopus 로고
    • Identification, purification and characterization of thermally stable lipase from rice bran, a new member of the (phospho) lipase family
    • Bhardwaj, K., Raju, A., & Rajasekharan, R. (2000). Identification, purification and characterization of thermally stable lipase from rice bran, a new member of the (phospho) lipase family. Plant Physiology,127, 1728–1738.
    • (2000) Plant Physiology , vol.127 , pp. 1728-1738
    • Bhardwaj, K.1    Raju, A.2    Rajasekharan, R.3
  • 2
    • 0028078789 scopus 로고
    • Cloning of the classical guinea pig pancreatic lipase and comparison with lipase related protein 2
    • PID: 8307159
    • Carrière, F., Thirstrup, K., Hjorth, S., & Boel, E. (1994). Cloning of the classical guinea pig pancreatic lipase and comparison with lipase related protein 2. FEBS Letters,338, 63–68.
    • (1994) FEBS Letters , vol.338 , pp. 63-68
    • Carrière, F.1    Thirstrup, K.2    Hjorth, S.3    Boel, E.4
  • 4
    • 33747518326 scopus 로고    scopus 로고
    • Industrial applications of microbial lipases
    • COI: 1:CAS:528:DC%2BD28XkslSksbc%3D
    • Hasan, F., Shah, A. A., & Hameed, A. (2006). Industrial applications of microbial lipases. Enzyme and Microbial Technology,39, 235–251.
    • (2006) Enzyme and Microbial Technology , vol.39 , pp. 235-251
    • Hasan, F.1    Shah, A.A.2    Hameed, A.3
  • 5
    • 19444381947 scopus 로고    scopus 로고
    • High-yielding purification of an organic solvent-tolerant lipase from Pseudomonas sp
    • COI: 1:CAS:528:DC%2BD2MXktleju7w%3D, PID: 15907872
    • Rahman, R. N., Baharum, S. N., Basri, M., & Salleh, A. B. (2005). High-yielding purification of an organic solvent-tolerant lipase from Pseudomonas sp. Analytical Biochemistry,341, 267–274.
    • (2005) Analytical Biochemistry , vol.341 , pp. 267-274
    • Rahman, R.N.1    Baharum, S.N.2    Basri, M.3    Salleh, A.B.4
  • 6
    • 0000233752 scopus 로고    scopus 로고
    • Lipase specificities: Potential applications in lipid bioconversions
    • Villeneuve, P., & Foglia, T. (1997). Lipase specificities: Potential applications in lipid bioconversions. Inform,8, 640–650.
    • (1997) Inform , vol.8 , pp. 640-650
    • Villeneuve, P.1    Foglia, T.2
  • 8
    • 20444408450 scopus 로고    scopus 로고
    • Characterization of thermostable lipase from thermophilic Geobacillus sp. TW1
    • PID: 15939301
    • Li, H., & Zhang, X. (2005). Characterization of thermostable lipase from thermophilic Geobacillus sp. TW1. Protein Expression and Purification,42, 153–159.
    • (2005) Protein Expression and Purification , vol.42 , pp. 153-159
    • Li, H.1    Zhang, X.2
  • 10
    • 0034731605 scopus 로고    scopus 로고
    • Lipase protein engineering
    • COI: 1:CAS:528:DC%2BD3MXitl2ltg%3D%3D, PID: 11150608
    • Svendsen, A. (2000). Lipase protein engineering. Biochimica et Biophysica Acta,1543, 223–238.
    • (2000) Biochimica et Biophysica Acta , vol.1543 , pp. 223-238
    • Svendsen, A.1
  • 11
    • 0344074507 scopus 로고    scopus 로고
    • Cloning, expression, characterization and role of leader sequence of lipase from Rhizopusoryzae
    • COI: 1:CAS:528:DyaK1cXltlegtLc%3D, PID: 9765593
    • Beer, H. D., McCathy, J. E., Borncheuer, U. T., & Schmidit, R. D. (1998). Cloning, expression, characterization and role of leader sequence of lipase from Rhizopusoryzae. Biochimica et Biophysica Acta,1399, 173–180.
    • (1998) Biochimica et Biophysica Acta , vol.1399 , pp. 173-180
    • Beer, H.D.1    McCathy, J.E.2    Borncheuer, U.T.3    Schmidit, R.D.4
  • 12
    • 0028448470 scopus 로고
    • Purification, characterization and crystallisation of two types of lipase from Rhizopus niveus
    • COI: 1:CAS:528:DyaK2cXlsFaqs7g%3D, PID: 7765029
    • Kohno, M., Kugimiya, W., Hashimoto, Y., & Morita, Y. (1994). Purification, characterization and crystallisation of two types of lipase from Rhizopus niveus. Bioscience, Biotechnology, and Biochemistry,58, 1007–1012.
    • (1994) Bioscience, Biotechnology, and Biochemistry , vol.58 , pp. 1007-1012
    • Kohno, M.1    Kugimiya, W.2    Hashimoto, Y.3    Morita, Y.4
  • 13
    • 0034927657 scopus 로고    scopus 로고
    • Kinetic study of Rhizopusoryzae using monomolecular film technique
    • Ben, Salah A., Sayarri, A., Verger, R., & Gargouri, Y. (2001). Kinetic study of Rhizopusoryzae using monomolecular film technique. Biochemie,83, 463–493.
    • (2001) Biochemie , vol.83 , pp. 463-493
    • Ben, S.A.1    Sayarri, A.2    Verger, R.3    Gargouri, Y.4
  • 15
    • 0017180966 scopus 로고
    • Interaction of pancreatic lipase with bile salts and dodecyl sulphate
    • COI: 1:CAS:528:DyaE28XlsFGltL0%3D
    • Borgstrom, B., & Donnér, J. (1976). Interaction of pancreatic lipase with bile salts and dodecyl sulphate. Lipid Research,17, 491–507.
    • (1976) Lipid Research , vol.17 , pp. 491-507
    • Borgstrom, B.1    Donnér, J.2
  • 16
    • 82155187076 scopus 로고    scopus 로고
    • A newly highly alkaline lipase: An ideal choice for application in detergent formulations
    • COI: 1:CAS:528:DC%2BC38XjsVaqsrg%3D, PID: 22123072
    • Cherif, S., Mnif, S., Hadrich, F., Abdelkafi, F., & Sayadi, S. (2011). A newly highly alkaline lipase: An ideal choice for application in detergent formulations. Lipids in Health and Disease,10, 221.
    • (2011) Lipids in Health and Disease , vol.10 , pp. 221
    • Cherif, S.1    Mnif, S.2    Hadrich, F.3    Abdelkafi, F.4    Sayadi, S.5
  • 17
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotator dispersion
    • COI: 1:CAS:528:DyaE3sXht12ltw%3D%3D, PID: 4343790
    • Chen, Y. H., Yang, J. T., & Martinez, H. (1972). Determination of the secondary structures of proteins by circular dichroism and optical rotator dispersion. Biochemistry,11, 4120–4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.3
  • 18
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsurprised learning neural network
    • COI: 1:CAS:528:DyaK3sXkvFSmsbg%3D, PID: 8332596
    • Andrade, M. A., Chacón, P., Merelo, J. J., & Morán, F. (1993). Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsurprised learning neural network. Protein Engineering,6, 383–390.
    • (1993) Protein Engineering , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 19
    • 33748363521 scopus 로고    scopus 로고
    • Characterization of partially folded intermediates of papain in presence of cationic, anionic and nonionic detergents at low pH
    • COI: 1:CAS:528:DC%2BD28XosFCqsrg%3D, PID: 16598711
    • Naeem, A., Fatima, S., & Khan, R. H. (2006). Characterization of partially folded intermediates of papain in presence of cationic, anionic and nonionic detergents at low pH. Biopolymers,83(1), 1–10.
    • (2006) Biopolymers , vol.83 , Issue.1 , pp. 1-10
    • Naeem, A.1    Fatima, S.2    Khan, R.H.3
  • 21
    • 33847659962 scopus 로고    scopus 로고
    • ANS fluorescence: potential to augment the identification of the external binding sites of proteins
    • COI: 1:CAS:528:DC%2BD2sXislWlsb8%3D, PID: 17321809
    • Gasymov, O. K., & Glasgow, B. J. (2007). ANS fluorescence: potential to augment the identification of the external binding sites of proteins. Biochimica et Biophysica Acta,1774, 403–411.
    • (2007) Biochimica et Biophysica Acta , vol.1774 , pp. 403-411
    • Gasymov, O.K.1    Glasgow, B.J.2
  • 22
    • 0002940127 scopus 로고
    • The molten globule State
    • Creighton TE, (ed), W. H. freeman, New York:
    • Ptisyn, O. B. (1992). The molten globule State. In T. E. Creighton (Ed.), Protein folding (pp. 243–300). New York: W. H. freeman.
    • (1992) Protein folding , pp. 243-300
    • Ptisyn, O.B.1
  • 23
    • 13444278724 scopus 로고    scopus 로고
    • Activation, inhibition and destabilization of Thermomyceslanuginosus lipase by detergents
    • COI: 1:CAS:528:DC%2BD2MXitVKhsg%3D%3D, PID: 15683256
    • Mogensen, J. E., Sehgal, P., & Otzen, D. E. (2005). Activation, inhibition and destabilization of Thermomyceslanuginosus lipase by detergents. Biochemistry,44, 1719–1730.
    • (2005) Biochemistry , vol.44 , pp. 1719-1730
    • Mogensen, J.E.1    Sehgal, P.2    Otzen, D.E.3
  • 25
    • 0034255687 scopus 로고    scopus 로고
    • Kinetics and mechanism of reactions catalysed by immobilized lipases
    • COI: 1:CAS:528:DC%2BD3cXkslSjtrw%3D, PID: 10899543
    • Paiva, A. L., Balca, V. M., & Malacta, F. X. (2000). Kinetics and mechanism of reactions catalysed by immobilized lipases. Enzyme and Microbial Technology,27, 187–204.
    • (2000) Enzyme and Microbial Technology , vol.27 , pp. 187-204
    • Paiva, A.L.1    Balca, V.M.2    Malacta, F.X.3
  • 26
    • 0029148636 scopus 로고
    • On the interfacial activation of Candida Antarctica lipase A and B as compared with Humicola lanuginosa lipase
    • Martinell, M., Holmquist, M., & Hulk, K. (1995). On the interfacial activation of Candida Antarctica lipase A and B as compared with Humicola lanuginosa lipase. Biochimica et Biophysica Acta,1258, 272–276.
    • (1995) Biochimica et Biophysica Acta , vol.1258 , pp. 272-276
    • Martinell, M.1    Holmquist, M.2    Hulk, K.3
  • 27
    • 0029898932 scopus 로고    scopus 로고
    • Lipase activation by non-ionic detergents, The crystal structure of the porcine lipase–colipasetetraethylene glycol monooctyl ether complex
    • Hermoso, J., Pignol, D., Kerfelec, B., Crenon, I., Chapus, C., & Fontecilla-Camps, J.-C. (1996). Lipase activation by non-ionic detergents, The crystal structure of the porcine lipase–colipasetetraethylene glycol monooctyl ether complex. Protein Journal of Biological Chemistry,271, 8007–80016.
    • (1996) Protein Journal of Biological Chemistry , vol.271 , pp. 8007-80016
    • Hermoso, J.1    Pignol, D.2    Kerfelec, B.3    Crenon, I.4    Chapus, C.5    Fontecilla-Camps, J.-C.6
  • 28
    • 0024086113 scopus 로고    scopus 로고
    • Catalytic activity and association of pancreatic lipase
    • Antonov, V. K., Dyakov, V. L., Mishin, A. A., & Rotanovo, T. V. (1998). Catalytic activity and association of pancreatic lipase. Biochimie,70, 1235–1244.
    • (1998) Biochimie , vol.70 , pp. 1235-1244
    • Antonov, V.K.1    Dyakov, V.L.2    Mishin, A.A.3    Rotanovo, T.V.4
  • 29
    • 2942558920 scopus 로고    scopus 로고
    • Activation and inhibition of Candida rugosa and Bacillus- related lipases by saturated fatty acids evaluated by new calorimetric microassay
    • COI: 1:CAS:528:DC%2BD2cXks1CjsL4%3D, PID: 15182938
    • Ruiz, C., Falcocchio, S., Xoxi, E., Pastor, F. I., Diaz, P., & Saso, L. (2004). Activation and inhibition of Candida rugosa and Bacillus- related lipases by saturated fatty acids evaluated by new calorimetric microassay. Biochimica et Biophysica Acta,1672, 184–191.
    • (2004) Biochimica et Biophysica Acta , vol.1672 , pp. 184-191
    • Ruiz, C.1    Falcocchio, S.2    Xoxi, E.3    Pastor, F.I.4    Diaz, P.5    Saso, L.6


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