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Volumn 3, Issue 3, 2014, Pages 77-82

Application of agriculture waste as a support for lipase immobilization

Author keywords

Acinetobacter baylyi; Adsorption; Agricultural waste; Lipase immobilization

Indexed keywords


EID: 84903739302     PISSN: 18788181     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcab.2014.02.002     Document Type: Article
Times cited : (35)

References (28)
  • 1
    • 0030088093 scopus 로고    scopus 로고
    • Immobilization of pectin lyase from Penicillium italicum by covalent binding to nylon
    • Alkorta I., Garbisu C., Llama M.J., Serra J.L. Immobilization of pectin lyase from Penicillium italicum by covalent binding to nylon. Enzyme Microb. Technol. 1996, 18:141-146.
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 141-146
    • Alkorta, I.1    Garbisu, C.2    Llama, M.J.3    Serra, J.L.4
  • 2
    • 0032486523 scopus 로고    scopus 로고
    • A single step purification, immobilization and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports
    • Bastida A., Sabuquillo P., Armisen P., Fernandez-Lafuente R., Huguet J., Guisan J.M. A single step purification, immobilization and hyperactivation of lipases via interfacial adsorption on strongly hydrophobic supports. Biotechnol. Bioeng. 1998, 58:486-493.
    • (1998) Biotechnol. Bioeng. , vol.58 , pp. 486-493
    • Bastida, A.1    Sabuquillo, P.2    Armisen, P.3    Fernandez-Lafuente, R.4    Huguet, J.5    Guisan, J.M.6
  • 3
    • 0028409645 scopus 로고
    • Blueprint for a lipase support use of hydrophobic controlled-pore glasses as model systems
    • Bosley J.A., Clayton J.C. Blueprint for a lipase support use of hydrophobic controlled-pore glasses as model systems. Biotechnol. Bioenergy 1994, 43:934-938.
    • (1994) Biotechnol. Bioenergy , vol.43 , pp. 934-938
    • Bosley, J.A.1    Clayton, J.C.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dry binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dry binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 84863186045 scopus 로고    scopus 로고
    • Biogas production from agricultural wastes in Thailand
    • Chaiprasert P. Biogas production from agricultural wastes in Thailand. J. Sustain. Energy Environ. 2011, 63-65.
    • (2011) J. Sustain. Energy Environ. , pp. 63-65
    • Chaiprasert, P.1
  • 6
    • 33947608859 scopus 로고    scopus 로고
    • Arthrobacter sp. Lipase immobilization for improvement in stability and enantioselectivity
    • (Special issue)
    • Chaubey A., Parshad R., Koul S., Taneja S.C., Qazi G.N. Arthrobacter sp. Lipase immobilization for improvement in stability and enantioselectivity. Appl. Microbiol. Biotechnol. 2006, 73(3):598-606. (Special issue).
    • (2006) Appl. Microbiol. Biotechnol. , vol.73 , Issue.3 , pp. 598-606
    • Chaubey, A.1    Parshad, R.2    Koul, S.3    Taneja, S.C.4    Qazi, G.N.5
  • 7
    • 80051793850 scopus 로고    scopus 로고
    • Enhancing the functional properties of the thermophilic enzymes by chemical modification and immobilization
    • Cowan D.A., Fernandez-Lafuente R. Enhancing the functional properties of the thermophilic enzymes by chemical modification and immobilization. Enzyme Microb. Technol. 2011, 49:326-346.
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 326-346
    • Cowan, D.A.1    Fernandez-Lafuente, R.2
  • 8
    • 1842834012 scopus 로고    scopus 로고
    • Immobilization of α-amylase from Bacillus circulans GRS 313 on coconut fiber
    • Dey G., Nagpal V., Banerjee R. Immobilization of α-amylase from Bacillus circulans GRS 313 on coconut fiber. Appl. Biochem. Biotechnol. 2002, 102-103:303-313.
    • (2002) Appl. Biochem. Biotechnol. , vol.102-103 , pp. 303-313
    • Dey, G.1    Nagpal, V.2    Banerjee, R.3
  • 9
    • 84903712989 scopus 로고    scopus 로고
    • European Environment Agency, What is waste-Chapter 2 Waste types, European topic centre on sustainable consumption and production, Copenhagen.
    • European Environment Agency, 2006. What is waste-Chapter 2 Waste types, European topic centre on sustainable consumption and production, Copenhagen.
    • (2006)
  • 10
    • 33751535398 scopus 로고    scopus 로고
    • A newly isolated organic solvent tolerant Staphylococcus saprophyticus M36 produced organic solvent-stable lipase
    • Fang Y., Lu Z., Lv F., Bie X., Liu S., Ding Z., Xu W. A newly isolated organic solvent tolerant Staphylococcus saprophyticus M36 produced organic solvent-stable lipase. Curr. Microbiol. 2006, 53:510-515.
    • (2006) Curr. Microbiol. , vol.53 , pp. 510-515
    • Fang, Y.1    Lu, Z.2    Lv, F.3    Bie, X.4    Liu, S.5    Ding, Z.6    Xu, W.7
  • 11
    • 68849108440 scopus 로고    scopus 로고
    • Enzymes from solvent-tolerant microbes: useful biocatalysts for non-aqueous enzymology
    • Gupta A., Khare S.K. Enzymes from solvent-tolerant microbes: useful biocatalysts for non-aqueous enzymology. Crit. Rev. Biotechnol. 2009, 29:44-54.
    • (2009) Crit. Rev. Biotechnol. , vol.29 , pp. 44-54
    • Gupta, A.1    Khare, S.K.2
  • 13
    • 84903735795 scopus 로고    scopus 로고
    • Office of Agricultural Economics, Agricultural statistics of Thailand, Ministry of Agriculture and Cooperatives, Bangkok, Thailand.
    • Office of Agricultural Economics, 2004. Agricultural statistics of Thailand, Ministry of Agriculture and Cooperatives, Bangkok, Thailand.
    • (2004)
  • 14
    • 0037458533 scopus 로고    scopus 로고
    • Resolution of (±)-5-substituted-6-(5-choloropyridin-2-yl)-7-oxo-5,6-dihydropyrrolo [3, 4b] pyrazine derivatives-precursors of S-(+)-Zopiclone, catalyzed by immobilized Candida antartica B lipase in aqueous media
    • Palomo J.M., Mateo C., Fernández-Lorente G., Solares L.F., Diaz M., Sánchez V.M., Bayod M., Gotor V., Guisana J.M., Fernández-Lafuente R. Resolution of (±)-5-substituted-6-(5-choloropyridin-2-yl)-7-oxo-5,6-dihydropyrrolo [3, 4b] pyrazine derivatives-precursors of S-(+)-Zopiclone, catalyzed by immobilized Candida antartica B lipase in aqueous media. Tetrahedron Asymmetry 2003, 14:429-438.
    • (2003) Tetrahedron Asymmetry , vol.14 , pp. 429-438
    • Palomo, J.M.1    Mateo, C.2    Fernández-Lorente, G.3    Solares, L.F.4    Diaz, M.5    Sánchez, V.M.6    Bayod, M.7    Gotor, V.8    Guisana, J.M.9    Fernández-Lafuente, R.10
  • 15
    • 0037010728 scopus 로고    scopus 로고
    • Interfacial adsorption of lipase on very hydrophobic support (octadecyl-Sepabeds): immobilization, hyperactivation and stabilization of the open form of lipases
    • Palomo J.M., Muñoz G., Fernández-Lorente G., Mateo C., Fernández-Lafuente R., Guisan J.M. Interfacial adsorption of lipase on very hydrophobic support (octadecyl-Sepabeds): immobilization, hyperactivation and stabilization of the open form of lipases. J. Mol. Catal. B 2002, 19:279-286.
    • (2002) J. Mol. Catal. B , vol.19 , pp. 279-286
    • Palomo, J.M.1    Muñoz, G.2    Fernández-Lorente, G.3    Mateo, C.4    Fernández-Lafuente, R.5    Guisan, J.M.6
  • 16
    • 0030152430 scopus 로고    scopus 로고
    • Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: a simple test for the determination of lipase activity in organic media
    • Pencreac'h G., Baratii J.C. Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: a simple test for the determination of lipase activity in organic media. Enzyme Microb. Technol. 1996, 18:417-422.
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 417-422
    • Pencreac'h, G.1    Baratii, J.C.2
  • 17
    • 33646467572 scopus 로고    scopus 로고
    • Immobilization of lipases for non-aqueous synthesis
    • Petkar M., Lali A., Caimi P., Daminati M. Immobilization of lipases for non-aqueous synthesis. J. Mol. Catal. B 2006, 39:83-90.
    • (2006) J. Mol. Catal. B , vol.39 , pp. 83-90
    • Petkar, M.1    Lali, A.2    Caimi, P.3    Daminati, M.4
  • 18
    • 29244438451 scopus 로고    scopus 로고
    • Biomass and biogas energy in Thailand: potential, opportunity and barriers
    • Prasertsan P., Sajjakulnukit B. Biomass and biogas energy in Thailand: potential, opportunity and barriers. Renew. Energy 2006, 31:599-610.
    • (2006) Renew. Energy , vol.31 , pp. 599-610
    • Prasertsan, P.1    Sajjakulnukit, B.2
  • 19
    • 0024278878 scopus 로고
    • The hydrolysis of triglycerides by immobilized lipase in a hydrophilic membrane reactor
    • Pronk W., Kerkhof P.J.A., van Helden C., Van't Reit K. The hydrolysis of triglycerides by immobilized lipase in a hydrophilic membrane reactor. Biotechnol. Bioeng. 1988, 32:512-518.
    • (1988) Biotechnol. Bioeng. , vol.32 , pp. 512-518
    • Pronk, W.1    Kerkhof, P.J.A.2    van Helden, C.3    Van't Reit, K.4
  • 20
    • 0036525716 scopus 로고    scopus 로고
    • Lipases as practical biocatalysts
    • Reetz M.T. Lipases as practical biocatalysts. Curr. Opin. Chem. Biol. 2002, 6:145-150.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 145-150
    • Reetz, M.T.1
  • 21
    • 17444452230 scopus 로고    scopus 로고
    • Characterization of Accurel MP1004 polypropylene powder and its use as support for lipase immobilization
    • Salis A., Sanjust E., Solinas V., Monduzzi M. Characterization of Accurel MP1004 polypropylene powder and its use as support for lipase immobilization. J. Mol. Catal. B 2003, 24-25:75-82.
    • (2003) J. Mol. Catal. B , vol.24-25 , pp. 75-82
    • Salis, A.1    Sanjust, E.2    Solinas, V.3    Monduzzi, M.4
  • 23
    • 0035991501 scopus 로고    scopus 로고
    • Tolerance of bacteria to organic solvent
    • Sardessai Y., Bhosle S. Tolerance of bacteria to organic solvent. Res. Microbiol. 2002, 153:263-268.
    • (2002) Res. Microbiol. , vol.153 , pp. 263-268
    • Sardessai, Y.1    Bhosle, S.2
  • 24
    • 79960528554 scopus 로고    scopus 로고
    • Nutritional requirements and physical factors affecting the production of organic solvent-stable lipase by Acinetobacter baylyi
    • Uttatree S., Charoenpanich J. Nutritional requirements and physical factors affecting the production of organic solvent-stable lipase by Acinetobacter baylyi. CMUJ. Nat. Sci. 2011, 10(1):115-131.
    • (2011) CMUJ. Nat. Sci. , vol.10 , Issue.1 , pp. 115-131
    • Uttatree, S.1    Charoenpanich, J.2
  • 25
    • 77955926979 scopus 로고    scopus 로고
    • Isolation and characterization of a novel thermophilic-organic solvent stable lipase from Acinetobacter baylyi
    • Uttatree S., Winayanuwattikun P., Charoenpanich J. Isolation and characterization of a novel thermophilic-organic solvent stable lipase from Acinetobacter baylyi. Appl. Biochem. Biotechnol. 2010, 162:1362-1376.
    • (2010) Appl. Biochem. Biotechnol. , vol.162 , pp. 1362-1376
    • Uttatree, S.1    Winayanuwattikun, P.2    Charoenpanich, J.3
  • 26
    • 0034697072 scopus 로고    scopus 로고
    • Customising lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches
    • Villeneuve P., Muderhwa J.M., Graille J., Haas M.J. Customising lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches. J. Mol. Catal. B 2000, 9:113-148.
    • (2000) J. Mol. Catal. B , vol.9 , pp. 113-148
    • Villeneuve, P.1    Muderhwa, J.M.2    Graille, J.3    Haas, M.J.4
  • 27
    • 33750605776 scopus 로고    scopus 로고
    • Lipase-catalyzed biodiesel production from soybean oil deodorizer distillate with adsorbent present in tert-butanol system
    • Wang L., Du W., Liu D., Li L., Dai N. Lipase-catalyzed biodiesel production from soybean oil deodorizer distillate with adsorbent present in tert-butanol system. J. Mol. Catal. B 2006, 43:29-32.
    • (2006) J. Mol. Catal. B , vol.43 , pp. 29-32
    • Wang, L.1    Du, W.2    Liu, D.3    Li, L.4    Dai, N.5
  • 28
    • 35449002498 scopus 로고    scopus 로고
    • Gene cloning, overexpression and characterization of a novel organic solvent tolerant and thermostable lipase from Galactomyces geotrichum Y05
    • Yan G., Yang G., Xu L., Yan Y. Gene cloning, overexpression and characterization of a novel organic solvent tolerant and thermostable lipase from Galactomyces geotrichum Y05. J. Mol. Catal. B 2007, 49:28-35.
    • (2007) J. Mol. Catal. B , vol.49 , pp. 28-35
    • Yan, G.1    Yang, G.2    Xu, L.3    Yan, Y.4


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