메뉴 건너뛰기




Volumn 86, Issue 6, 2011, Pages 838-844

On the hyperthermostability of lipolytic enzymes from Thermus aquaticus YT-1: Exploring their application to polymer degradation

Author keywords

Enzyme; Lipolytic activity; Polymer degradation; Themostability; Thermophiles; Thermus aquaticus YT1

Indexed keywords

LIPOLYTIC ACTIVITY; POLYMER DEGRADATION; THEMOSTABILITY; THERMOPHILES; THERMUS AQUATICUS;

EID: 79955967117     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.2597     Document Type: Article
Times cited : (3)

References (43)
  • 1
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • Jaeger KE and Reetz MT, Microbial lipases form versatile tools for biotechnology. Trends Biotechnol 16: 396-403 (1998).
    • (1998) Trends Biotechnol , vol.16 , pp. 396-403
    • Jaeger, K.E.1    Reetz, M.T.2
  • 4
    • 77957852691 scopus 로고    scopus 로고
    • Lipases from the genus Penicillium: production, purification, characterization and applications
    • Li N and Zong MH, Lipases from the genus Penicillium: production, purification, characterization and applications. J Mol Catal B-Enzym 66: 43-54 (2010).
    • (2010) J Mol Catal B-Enzym , vol.66 , pp. 43-54
    • Li, N.1    Zong, M.H.2
  • 5
    • 77951498332 scopus 로고    scopus 로고
    • Lipase from Rhizomucor miehei as an industrial biocatalyst in chemical process
    • Rodrigues RC and Fernandez-Lafuente R, Lipase from Rhizomucor miehei as an industrial biocatalyst in chemical process J Mol Catal B-Enzym 64: 1-22 (2010).
    • (2010) J Mol Catal B-Enzym , vol.64 , pp. 1-22
    • Rodrigues, R.C.1    Fernandez-Lafuente, R.2
  • 9
    • 61549106933 scopus 로고    scopus 로고
    • Thermus thermophilus as biological model
    • Cava F, Hidalgo A and Berenguer J, Thermus thermophilus as biological model. Extremophiles 13: 213-231 (2009).
    • (2009) Extremophiles , vol.13 , pp. 213-231
    • Cava, F.1    Hidalgo, A.2    Berenguer, J.3
  • 10
    • 0014501198 scopus 로고
    • Thermus aquaticus gen. n. and sp. n., a non-sporulating extreme thermophile
    • Brock TD and Freeze H, Thermus aquaticus gen. n. and sp. n., a non-sporulating extreme thermophile. J Bacteriol 98: 289-297 (1969).
    • (1969) J Bacteriol , vol.98 , pp. 289-297
    • Brock, T.D.1    Freeze, H.2
  • 11
    • 0028829580 scopus 로고
    • Identification of new enzyme activities of several strains of Thermus species
    • Berger JL, Lee BH and Lacroix C, Identification of new enzyme activities of several strains of Thermus species. Appl Microbiol Biotechnol 44: 81-87 (1995).
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 81-87
    • Berger, J.L.1    Lee, B.H.2    Lacroix, C.3
  • 12
    • 3342883774 scopus 로고    scopus 로고
    • Quantification of intra- and extra- cellular thermophilic lipase/esterase production by Thermus spp
    • Domínguez A, Sanromán MA, Fuciños P, Rúa ML, Pastrana L and Longo MA, Quantification of intra- and extra- cellular thermophilic lipase/esterase production by Thermus spp. Biotechnol Lett 26: 705-708 (2004).
    • (2004) Biotechnol Lett , vol.26 , pp. 705-708
    • Domínguez, A.1    Sanromán, M.A.2    Fuciños, P.3    Rúa, M.L.4    Pastrana, L.5    Longo, M.A.6
  • 14
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille C and Zeikus G, Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65: 1-43 (2001).
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.2
  • 16
    • 57749192729 scopus 로고    scopus 로고
    • Degradation of a terephthalate-containing polyester by thermophilic Actinomycetes and Bacillus species derived from composts
    • Hu XP, Osaki S, Hayashi M, Kaku M, Katuen S, Kobayashi H, et al, Degradation of a terephthalate-containing polyester by thermophilic Actinomycetes and Bacillus species derived from composts. J Polym Env 16: 103-108 (2008).
    • (2008) J Polym Env , vol.16 , pp. 103-108
    • Hu, X.P.1    Osaki, S.2    Hayashi, M.3    Kaku, M.4    Katuen, S.5    Kobayashi, H.6
  • 17
    • 34548170495 scopus 로고    scopus 로고
    • Polyester-degrading thermophilic actinomycetes isolated from different environment in Taiwan
    • Tseng M, Hoang KC, Yang MK, Yang SF and Chu WS, Polyester-degrading thermophilic actinomycetes isolated from different environment in Taiwan. Biodegradation 18: 579-583 (2007).
    • (2007) Biodegradation , vol.18 , pp. 579-583
    • Tseng, M.1    Hoang, K.C.2    Yang, M.K.3    Yang, S.F.4    Chu, W.S.5
  • 19
    • 18144402872 scopus 로고    scopus 로고
    • Identification of extracellular lipases/esterases produced by Thermus thermophilus HB27: partial purification and preliminary biochemical characterisation
    • Fuciños P, Abadín CM, Sanromán MA, Longo MA, Pastrana L and Rúa ML, Identification of extracellular lipases/esterases produced by Thermus thermophilus HB27: partial purification and preliminary biochemical characterisation. J Biotechnol 117: 233-241 (2005).
    • (2005) J Biotechnol , vol.117 , pp. 233-241
    • Fuciños, P.1    Abadín, C.M.2    Sanromán, M.A.3    Longo, M.A.4    Pastrana, L.5    Rúa, M.L.6
  • 20
    • 2642584964 scopus 로고    scopus 로고
    • A novel phospholipase A(2)/esterase from hyperthermophilic archaeon Aeropyrum pernix K-1
    • Wang BJ, Lu DM, Gao RJ, Yang Z, Cao SG and Feng Y, A novel phospholipase A(2)/esterase from hyperthermophilic archaeon Aeropyrum pernix K-1. Protein Expr Purif 35: 199-205 (2004).
    • (2004) Protein Expr Purif , vol.35 , pp. 199-205
    • Wang, B.J.1    Lu, D.M.2    Gao, R.J.3    Yang, Z.4    Cao, S.G.5    Feng, Y.6
  • 21
    • 0342646950 scopus 로고    scopus 로고
    • Characterization of a newthermostable esterase from themoderate thermophilic bacterium Bacillus circulans
    • Kademi A, Ait-Abdelkader N, Fakhreddine L and Baratti JC, Characterization of a newthermostable esterase from themoderate thermophilic bacterium Bacillus circulans. J Mol Catal B-Enzym 10: 395-401 (2000).
    • (2000) J Mol Catal B-Enzym , vol.10 , pp. 395-401
    • Kademi, A.1    Ait-Abdelkader, N.2    Fakhreddine, L.3    Baratti, J.C.4
  • 22
    • 31044448437 scopus 로고    scopus 로고
    • A novel esterase from Bacillus subtilis (RRL 1789): purification and characterization of the enzyme
    • Kaiser P, Raina C, Parshad R, Johri S, Verma V, Andrabi KI, et al, A novel esterase from Bacillus subtilis (RRL 1789): purification and characterization of the enzyme. Protein Expr Purif 45: 262-268 (2006).
    • (2006) Protein Expr Purif , vol.45 , pp. 262-268
    • Kaiser, P.1    Raina, C.2    Parshad, R.3    Johri, S.4    Verma, V.5    Andrabi, K.I.6
  • 25
    • 70449403245 scopus 로고    scopus 로고
    • Evaluation of a novel Bacillus strain from a north-western Spain hot spring as a source of extracellular thermostable lipase
    • Deive FJ, Sanromán MA and Longo MA, Evaluation of a novel Bacillus strain from a north-western Spain hot spring as a source of extracellular thermostable lipase. J Chem Technol Biotechnol 84: 1509-1515 (2009).
    • (2009) J Chem Technol Biotechnol , vol.84 , pp. 1509-1515
    • Deive, F.J.1    Sanromán, M.A.2    Longo, M.A.3
  • 26
    • 33847113881 scopus 로고    scopus 로고
    • Characterization of a thermostable carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima
    • Kakugawa S, Fushinobu S, Wakagi T and Shoun H, Characterization of a thermostable carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima. Appl Microbiol Biotechnol 74: 585-591 (2007).
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 585-591
    • Kakugawa, S.1    Fushinobu, S.2    Wakagi, T.3    Shoun, H.4
  • 27
    • 34247598789 scopus 로고    scopus 로고
    • A new phosphotriesterase from Sulfolobus acidocaldarius and its comparison with the homologue from Sulfolobus solfataricus
    • Porzio E, Merone L, Mandrich L, Rossi M and Manco G, A new phosphotriesterase from Sulfolobus acidocaldarius and its comparison with the homologue from Sulfolobus solfataricus. Biochimie 89: 625-636 (2007).
    • (2007) Biochimie , vol.89 , pp. 625-636
    • Porzio, E.1    Merone, L.2    Mandrich, L.3    Rossi, M.4    Manco, G.5
  • 28
    • 34547643363 scopus 로고    scopus 로고
    • Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties
    • Byun JS, Rhee JK, Kim ND, Yoon JH, Kim DU, Koh E, et al, Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties. BMC Struct Biol 7: 47-58 (2007).
    • (2007) BMC Struct Biol , vol.7 , pp. 47-58
    • Byun, J.S.1    Rhee, J.K.2    Kim, N.D.3    Yoon, J.H.4    Kim, D.U.5    Koh, E.6
  • 29
    • 0025876117 scopus 로고
    • A chaperonin from a thermophilic bacterium, Thermus thermophilus, that controls refoldings of several thermophilic enzyme
    • Taguchi H, Konishi J, Ishii N and Yoshida M, A chaperonin from a thermophilic bacterium, Thermus thermophilus, that controls refoldings of several thermophilic enzyme. J Biol Chem 266: 22411-22418 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 22411-22418
    • Taguchi, H.1    Konishi, J.2    Ishii, N.3    Yoshida, M.4
  • 30
    • 0022013872 scopus 로고
    • Categorization of enzyme deactivations using a series-type mechanism
    • Henley JP and Sadana A, Categorization of enzyme deactivations using a series-type mechanism. Enzyme Microb Technol 7: 50-60 (1985).
    • (1985) Enzyme Microb Technol , vol.7 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2
  • 31
    • 0033003960 scopus 로고    scopus 로고
    • Thermostability of modified enzymes: a detailed study
    • Longo MA and Combes D, Thermostability of modified enzymes: a detailed study. J Chem Technol Biotechnol 74: 25-32 (1999).
    • (1999) J Chem Technol Biotechnol , vol.74 , pp. 25-32
    • Longo, M.A.1    Combes, D.2
  • 32
    • 10744230827 scopus 로고    scopus 로고
    • Some like it cold: biocatalysis at low temperatures
    • Georlette D, Blaise V and Collins T, Some like it cold: biocatalysis at low temperatures. FEMS Microbiol Rev 28: 25-42 (2004).
    • (2004) FEMS Microbiol Rev , vol.28 , pp. 25-42
    • Georlette, D.1    Blaise, V.2    Collins, T.3
  • 33
    • 0029134288 scopus 로고
    • The effect of polyol compounds on the thermostability of penicillin G acylase from a mutant of Escherichia coli ATCC 11105
    • Erarslan A, The effect of polyol compounds on the thermostability of penicillin G acylase from a mutant of Escherichia coli ATCC 11105. Process Biochem 30: 133-139 (1995).
    • (1995) Process Biochem , vol.30 , pp. 133-139
    • Erarslan, A.1
  • 34
    • 0030271204 scopus 로고    scopus 로고
    • Comparative thermostability of glucose dehydrogenase from Haloferax mediterranei. Effects of salts and polyols
    • Obón JM, Manjón A and Iborra JL, Comparative thermostability of glucose dehydrogenase from Haloferax mediterranei. Effects of salts and polyols. Enzyme Microbiol Technol 19: 352-360 (1996).
    • (1996) Enzyme Microbiol Technol , vol.19 , pp. 352-360
    • Obón, J.M.1    Manjón, A.2    Iborra, J.L.3
  • 35
    • 73449104308 scopus 로고    scopus 로고
    • Thermal stability of α-amylase in aqueous cosolvent systems
    • Yadav JK and Prakash V, Thermal stability of α-amylase in aqueous cosolvent systems. J Biosci 34: 377-387 (2009).
    • (2009) J Biosci , vol.34 , pp. 377-387
    • Yadav, J.K.1    Prakash, V.2
  • 36
    • 57349088622 scopus 로고    scopus 로고
    • Influence of polyols on the stability and kinetic parameters of invertase from Candida utilis: correlation with the conformational stability and activity
    • Gangadhara, Ramesh Kumar P and Prakash V, Influence of polyols on the stability and kinetic parameters of invertase from Candida utilis: correlation with the conformational stability and activity. Protein J 27: 440-449 (2008).
    • (2008) Protein J , vol.27 , pp. 440-449
    • Gangadhara1    Ramesh Kumar, P.2    Prakash, V.3
  • 37
    • 0017764090 scopus 로고
    • Hydrolisis of polyesters by lipases
    • Tokiwa Y and Suzuki T, Hydrolisis of polyesters by lipases. Nature 270: 76-78 (1977).
    • (1977) Nature , vol.270 , pp. 76-78
    • Tokiwa, Y.1    Suzuki, T.2
  • 38
    • 0006063437 scopus 로고    scopus 로고
    • Enzymatic degradation of poly(ethylene terephthalate) copolymers with aliphatic dicarboxylic acids and/or poly(ethylene glycol)
    • Nagata M, Kitotsukuri T, Minami S, Tsutsumi N and Sakai W, Enzymatic degradation of poly(ethylene terephthalate) copolymers with aliphatic dicarboxylic acids and/or poly(ethylene glycol). Eur Polym J 33: 1701-1705 (1997).
    • (1997) Eur Polym J , vol.33 , pp. 1701-1705
    • Nagata, M.1    Kitotsukuri, T.2    Minami, S.3    Tsutsumi, N.4    Sakai, W.5
  • 39
    • 0037058061 scopus 로고    scopus 로고
    • Characterization and degradation behavior of poly(butylene adipate-co-terephthalate)s
    • Herrera R, Franco L, Rodríguez-Galan A and Puiggali JJ, Characterization and degradation behavior of poly(butylene adipate-co-terephthalate)s. Polym Sci Polym Chem 40: 4141-4157 (2002).
    • (2002) Polym Sci Polym Chem , vol.40 , pp. 4141-4157
    • Herrera, R.1    Franco, L.2    Rodríguez-Galan, A.3    Puiggali, J.J.4
  • 40
  • 41
    • 1542268883 scopus 로고    scopus 로고
    • Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents
    • Lima VMG, Krieger N, Mitchell DA and Fontana LD, Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents. Biochem Eng J 18: 65-71 (2004).
    • (2004) Biochem Eng J , vol.18 , pp. 65-71
    • Lima, V.M.G.1    Krieger, N.2    Mitchell, D.A.3    Fontana, L.D.4
  • 42
    • 0032127057 scopus 로고    scopus 로고
    • Effect of detergents on activity of microbial lipases as measured by the nitrophenyl alkanoate esters method
    • Helistöa P and Korpela T, Effect of detergents on activity of microbial lipases as measured by the nitrophenyl alkanoate esters method. Enzyme Microbiol Technol 23: 113-117 (1998).
    • (1998) Enzyme Microbiol Technol , vol.23 , pp. 113-117
    • Helistöa, P.1    Korpela, T.2
  • 43


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.