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Volumn 40, Issue 2, 2013, Pages 217-226

A low molecular mass cutinase of Thielavia terrestris efficiently hydrolyzes poly(esters)

Author keywords

Characterization; Cutinase; Ester polymer degradation; Organic solvent; Thielavia terrestris

Indexed keywords

2 PROPANOL; ACETONE; ACETONITRILE; ALCOHOL; CUTINASE; DIMETHYL SULFOXIDE; METHANOL; POLYCAPROLACTONE; POLYESTER; POLYETHYLENE TEREPHTHALATE;

EID: 84878472865     PISSN: 13675435     EISSN: 14765535     Source Type: Journal    
DOI: 10.1007/s10295-012-1222-x     Document Type: Article
Times cited : (75)

References (48)
  • 1
    • 84856276820 scopus 로고    scopus 로고
    • Identification and comparison of cutinases for synthetic polyester degradation
    • 21713515 10.1007/s00253-011-3402-4
    • Baker PJ, Poultney C, Liu Z, Gross R, Montclare JK (2012) Identification and comparison of cutinases for synthetic polyester degradation. Appl Microbiol Biotechnol 93:229-240
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 229-240
    • Baker, P.J.1    Poultney, C.2    Liu, Z.3    Gross, R.4    Montclare, J.K.5
  • 2
    • 70149108283 scopus 로고    scopus 로고
    • From petrochemical complexes to biorefineries? the past and prospective co-evolution of liquid fuel and chemicals production in the UK
    • 10.1016/j.cherd.2009.02.008 1:CAS:528:DC%2BD1MXht1GjtrrL
    • Bennett SJ, Pearson PJG (2009) From petrochemical complexes to biorefineries? The past and prospective co-evolution of liquid fuel and chemicals production in the UK. Chem Eng Res Des 87:1120-1139
    • (2009) Chem Eng Res des , vol.87 , pp. 1120-1139
    • Bennett, S.J.1    Pearson, P.J.G.2
  • 4
    • 77955550271 scopus 로고    scopus 로고
    • Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a carboxylesterase from Thermobifida fusca KW3
    • 20467738 10.1007/s00253-010-2635-y 1:CAS:528:DC%2BC3cXoslantbk%3D
    • Billig S, Oeser T, Birkemeyer C, Zimmermann W (2010) Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a carboxylesterase from Thermobifida fusca KW3. Appl Microbiol Biotechnol 87:1753-1764
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 1753-1764
    • Billig, S.1    Oeser, T.2    Birkemeyer, C.3    Zimmermann, W.4
  • 5
    • 0033230644 scopus 로고    scopus 로고
    • Cutinase: From molecular level to bioprocess development
    • 10556791 10.1002/(SICI)1097-0290(1999)66:1<17: AID-BIT2>3.0.CO;2-F 1:CAS:528:DyaK1MXnslKqsr0%3D
    • Carvalho CML, Aries-Barros MR, Cabral JMS (1999) Cutinase: from molecular level to bioprocess development. Biotechnol Bioeng 66:17-34
    • (1999) Biotechnol Bioeng , vol.66 , pp. 17-34
    • Carvalho, C.M.L.1    Aries-Barros, M.R.2    Cabral, J.M.S.3
  • 7
    • 77949540160 scopus 로고    scopus 로고
    • Biochemical characterization of cutinases from Thermobifida fusca
    • 10.1016/j.molcatb.2010.01.001
    • Chen S, Su LQ, Billig S, Zimmermann W, Chen J, Wu J (2011) Biochemical characterization of cutinases from Thermobifida fusca. J Mol Catal B Enzym 63:121-127
    • (2011) J Mol Catal B Enzym , vol.63 , pp. 121-127
    • Chen, S.1    Su, L.Q.2    Billig, S.3    Zimmermann, W.4    Chen, J.5    Wu, J.6
  • 8
    • 54449102399 scopus 로고    scopus 로고
    • Identification and characterization of bacterial cutinase
    • 18658138 10.1074/jbc.M800848200 1:CAS:528:DC%2BD1cXhtFSltLrN
    • Chen S, Tong X, Woodard RW, Du G, Wu J, Chen J (2008) Identification and characterization of bacterial cutinase. J Biol Chem 283:25854-25862
    • (2008) J Biol Chem , vol.283 , pp. 25854-25862
    • Chen, S.1    Tong, X.2    Woodard, R.W.3    Du, G.4    Wu, J.5    Chen, J.6
  • 9
    • 33846176102 scopus 로고    scopus 로고
    • Purification and identification of cutianses from Colletotrichum kahawae and Colletotrichum gloeosporioides
    • Chen ZJ, Franco CF, Baptista RP, Cabral MS, Coelho AV (2007) Purification and identification of cutianses from Colletotrichum kahawae and Colletotrichum gloeosporioides. Appl Microbiol Biotechnol 73:1313-1360
    • (2007) Appl Microbiol Biotechnol , vol.73 , pp. 1313-1360
    • Chen, Z.J.1    Franco, C.F.2    Baptista, R.P.3    Cabral, M.S.4    Coelho, A.V.5
  • 10
    • 0033762099 scopus 로고    scopus 로고
    • A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase
    • Eggert T, Pencreaćh G, Douchet I, Verger R, Jaeger KE (2000) A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase. Eur J Biochem 267:6459-6469
    • (2000) Eur J Biochem , vol.267 , pp. 6459-6469
    • Eggert, T.1    Pencreaćh, G.2    Douchet, I.3    Verger, R.4    Jaeger, K.E.5
  • 11
    • 0032957361 scopus 로고    scopus 로고
    • Production of cutinase by Thermomonospora fusca ATCC 27730
    • 10.1046/j.1365-2672.1999.00690.x 1:CAS:528:DyaK1MXivVCmsbk%3D
    • Fett WF, Wijey C, Moreau RA, Osman SF (1999) Production of cutinase by Thermomonospora fusca ATCC 27730. J Appl Microbiol 86:561-568
    • (1999) J Appl Microbiol , vol.86 , pp. 561-568
    • Fett, W.F.1    Wijey, C.2    Moreau, R.A.3    Osman, S.F.4
  • 12
    • 84856217875 scopus 로고    scopus 로고
    • Production of cutinase by Fusarium oxysporum on Brazilian agricultural by-products and its enantioselective properties
    • 10.1007/s11947-009-0261-4 1:CAS:528:DC%2BC38XhsV2nt7o%3D
    • Fraga LP, Carvalho PO, Macedo GA (2012) Production of cutinase by Fusarium oxysporum on Brazilian agricultural by-products and its enantioselective properties. Food Bioprocess Technol 5:138-146
    • (2012) Food Bioprocess Technol , vol.5 , pp. 138-146
    • Fraga, L.P.1    Carvalho, P.O.2    MacEdo, G.A.3
  • 13
    • 0026799608 scopus 로고
    • Characterization of the enzymes present in the cellulase system of Thielavia terrestris 255B
    • 10.1016/0960-8524(92)90134-J 1:CAS:528:DyaK38XltVKrur4%3D
    • Gilbert M, Breuil C, Saddler JN (1992) Characterization of the enzymes present in the cellulase system of Thielavia terrestris 255B. Bioresour Technol 39:147-153
    • (1992) Bioresour Technol , vol.39 , pp. 147-153
    • Gilbert, M.1    Breuil, C.2    Saddler, J.N.3
  • 14
    • 0026829935 scopus 로고
    • Purification and characterization of a xylanase from the thermophilic ascomycete Thielavia terrestris 255B
    • 1622204 10.1007/BF02920549
    • Gilbert M, Breuil C, Yaguchi M, Saddler JN (1992) Purification and characterization of a xylanase from the thermophilic ascomycete Thielavia terrestris 255B. Appl Biochem Biotechnol 34:247-259
    • (1992) Appl Biochem Biotechnol , vol.34 , pp. 247-259
    • Gilbert, M.1    Breuil, C.2    Yaguchi, M.3    Saddler, J.N.4
  • 15
    • 0036324633 scopus 로고    scopus 로고
    • Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon
    • 12147492 10.1128/AEM.68.8.3925-3931.2002 1:CAS:528:DC%2BD38XmtVejsr8%3D
    • Hotta Y, Ezaki S, Atomi H, Imanaka T (2002) Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon. Appl Environ Microbiol 68:3925-3931
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3925-3931
    • Hotta, Y.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 16
    • 0028360865 scopus 로고
    • A thermophilic, lopolytic Bacillus sp., and continous assay of its p-nitrophenyl palmitate esterase activity
    • 10.1111/j.1574-6968.1994.tb07030.x 1:CAS:528:DyaK2cXmsV2jtr0%3D
    • Janssen PH, Monk CR, Morgan HW (1994) A thermophilic, lopolytic Bacillus sp., and continous assay of its p-nitrophenyl palmitate esterase activity. FEMS Microbiol Lett 120:195-200
    • (1994) FEMS Microbiol Lett , vol.120 , pp. 195-200
    • Janssen, P.H.1    Monk, C.R.2    Morgan, H.W.3
  • 17
    • 79957503978 scopus 로고    scopus 로고
    • A novel family VII esterase with industrial potential from compost metagenomic library
    • 21619698 10.1186/1475-2859-10-41 1:CAS:528:DC%2BC3MXntlekurY%3D
    • Kang CH, Oh KH, Lee MH, Oh TK, Kim BH, Yoon JH (2011) A novel family VII esterase with industrial potential from compost metagenomic library. Microb Cell Fact 10:41
    • (2011) Microb Cell Fact , vol.10 , pp. 41
    • Kang, C.H.1    Oh, K.H.2    Lee, M.H.3    Oh, T.K.4    Kim, B.H.5    Yoon, J.H.6
  • 18
    • 17444408485 scopus 로고    scopus 로고
    • Cloning, recombinant expression and biochemical characterization of novel esterases from Bacillus sp. assoiated with the marine sponge Aplysina aerophoba
    • 15614567 10.1007/s00253-004-1780-6 1:CAS:528:DC%2BD2MXksFagtr8%3D
    • Karpushova A, Brümmer F, Barth S, Lange S, Schmid RD (2005) Cloning, recombinant expression and biochemical characterization of novel esterases from Bacillus sp. assoiated with the marine sponge Aplysina aerophoba. Appl Microbiol Biotechnol 67:59-69
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 59-69
    • Karpushova, A.1    Brümmer, F.2    Barth, S.3    Lange, S.4    Schmid, R.D.5
  • 19
    • 84863418333 scopus 로고    scopus 로고
    • Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolution
    • 10.1016/j.polymdegradstab.2012.02.003 1:CAS:528:DC%2BC38Xjt1elsrY%3D
    • Kitadokoro K, Thumarat U, Nakamura R, Nishimura K, Karatani H, Suzuki H, Kawai F (2012) Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolution. Polym Deg Stab 97:771-775
    • (2012) Polym Deg Stab , vol.97 , pp. 771-775
    • Kitadokoro, K.1    Thumarat, U.2    Nakamura, R.3    Nishimura, K.4    Karatani, H.5    Suzuki, H.6    Kawai, F.7
  • 20
    • 77955659882 scopus 로고    scopus 로고
    • Heterologous expression, characterization and site-directed mutagenesis of cutinase CUTAB 1 from Alternaria brassicicola
    • 20306187 10.1007/s00253-010-2533-3 1:CAS:528:DC%2BC3cXnsFGmtbs%3D
    • Koschorreck K, Liu D, Kazenwadel C, Schmid RD, Hauer B (2010) Heterologous expression, characterization and site-directed mutagenesis of cutinase CUTAB 1 from Alternaria brassicicola. Appl Microbiol Biotechnol 87:991-997
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 991-997
    • Koschorreck, K.1    Liu, D.2    Kazenwadel, C.3    Schmid, R.D.4    Hauer, B.5
  • 21
    • 51249167863 scopus 로고
    • Isolation and properties of a thermostable endoglucanase from a thermophilic mutant strain of Tielavia terrestris
    • 10.1007/BF02783450 1:CAS:528:DyaK2MXkt1ajt7k%3D
    • Kvesitadze EG, Lomitashvili TB, Khutsishvili MP, Lamed R, Bayer EA (1995) Isolation and properties of a thermostable endoglucanase from a thermophilic mutant strain of Tielavia terrestris. Appl Biochem Biotechnol 50:137-143
    • (1995) Appl Biochem Biotechnol , vol.50 , pp. 137-143
    • Kvesitadze, E.G.1    Lomitashvili, T.B.2    Khutsishvili, M.P.3    Lamed, R.4    Bayer, E.A.5
  • 22
    • 68349133480 scopus 로고    scopus 로고
    • High-level expression and characterization of Fusarium solani cutinase in Pichia pastoris
    • 10.1016/j.pep.2009.06.021 1:CAS:528:DC%2BD1MXhtVSmtrnN
    • Kwon MA, Kim HS, Yang TH, Song BK, Song JK (2009) High-level expression and characterization of Fusarium solani cutinase in Pichia pastoris. Portein Express Purif 68:104-109
    • (2009) Portein Express Purif , vol.68 , pp. 104-109
    • Kwon, M.A.1    Kim, H.S.2    Yang, T.H.3    Song, B.K.4    Song, J.K.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 70350633203 scopus 로고    scopus 로고
    • Structure and functional studies of Aspergillus oryzae cutinase: Enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation
    • 19810726 10.1021/ja9046697 1:CAS:528:DC%2BD1MXht1artLrF
    • Liu ZQ, Gosser YY, Baker PJ, Ravee Y (2009) Structure and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation. J Am Chem Soc 131:15711-15716
    • (2009) J Am Chem Soc , vol.131 , pp. 15711-15716
    • Liu, Z.Q.1    Gosser, Y.Y.2    Baker, P.J.3    Ravee, Y.4
  • 26
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • 14907713 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265-275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 28
    • 0025108631 scopus 로고
    • Effect of Tween 80 on the growth of Mycobacterium avium complex
    • 2280723 1:CAS:528:DyaK3MXjtlWq
    • Masaki S, Sugimori G, Okamoto A, Imose J, Hayashi Y (1990) Effect of Tween 80 on the growth of Mycobacterium avium complex. Microbiol Immunol 34:653-663
    • (1990) Microbiol Immunol , vol.34 , pp. 653-663
    • Masaki, S.1    Sugimori, G.2    Okamoto, A.3    Imose, J.4    Hayashi, Y.5
  • 29
    • 0001374815 scopus 로고
    • Biodegradable materials: Balancing degradability and performance
    • 1:CAS:528:DyaK2MXis1OhtQ%3D%3D
    • Mayer JM, Kaplin DL (1994) Biodegradable materials: balancing degradability and performance. Trends Polym Sci 2:227-235
    • (1994) Trends Polym Sci , vol.2 , pp. 227-235
    • Mayer, J.M.1    Kaplin, D.L.2
  • 30
    • 68949197248 scopus 로고    scopus 로고
    • Purification and identification of a novel cutinase from Coprinopsis cinerea by adsorptive bubble separation
    • 10.1016/j.seppur.2009.06.021 1:CAS:528:DC%2BD1MXhtVKntLvM
    • Merz J, Schembecker G, Riemer S, Nimtzc M, Zornb H (2009) Purification and identification of a novel cutinase from Coprinopsis cinerea by adsorptive bubble separation. Sep Purif Technol 69:57-62
    • (2009) Sep Purif Technol , vol.69 , pp. 57-62
    • Merz, J.1    Schembecker, G.2    Riemer, S.3    Nimtzc, M.4    Zornb, H.5
  • 31
    • 70349787145 scopus 로고    scopus 로고
    • Screening Botryosphaeria species for lipases: Production of lipase by Botryosphaeria ribis EC-01 grown on soybean oil and other carbon sources
    • 10.1016/j.enzmictec.2009.08.013 1:CAS:528:DC%2BD1MXht1GksLrN
    • Messias JM, da Costaa BZ, de Lima Valéria MG, Dekkerc RFH, Rezende MI, Krieger N, Barbosa AM (2009) Screening Botryosphaeria species for lipases: production of lipase by Botryosphaeria ribis EC-01 grown on soybean oil and other carbon sources. Enzyme Microb Technol 45:426-431
    • (2009) Enzyme Microb Technol , vol.45 , pp. 426-431
    • Messias, J.M.1    Da Costaa, B.Z.2    De Lima Valéria, M.G.3    Dekkerc, R.F.H.4    Rezende, M.I.5    Krieger, N.6    Barbosa, A.M.7
  • 32
    • 61449136037 scopus 로고    scopus 로고
    • The second green revolution? Production of plant based biodegradable plastics
    • 19196243 10.1042/BJ20081769 1:CAS:528:DC%2BD1MXhs1Ogu78%3D
    • Mooney BP (2009) The second green revolution? Production of plant based biodegradable plastics. Biochem J 418:219-232
    • (2009) Biochem J , vol.418 , pp. 219-232
    • Mooney, B.P.1
  • 33
    • 24944479050 scopus 로고    scopus 로고
    • Enzymatic degradation of poly(ethylene terephthalate): Rapid hydrolysis using a hydrolase from Thermobifida fusca
    • 10.1002/marc.200500410
    • Muller RJ, Schrader H, Profe J, Dresler K, Deckwer WD (2005) Enzymatic degradation of poly(ethylene terephthalate): rapid hydrolysis using a hydrolase from Thermobifida fusca. Macromol Rapid Commun 26:1400-1405
    • (2005) Macromol Rapid Commun , vol.26 , pp. 1400-1405
    • Muller, R.J.1    Schrader, H.2    Profe, J.3    Dresler, K.4    Deckwer, W.D.5
  • 34
    • 34047201827 scopus 로고    scopus 로고
    • Thermal stability of Humicola insolens cutinase in aqueous SDS
    • 10.1021/jp0709860 1:CAS:528:DC%2BD2sXitVCnur0%3D
    • Nielsen A, Borch K, Westh P (2007) Thermal stability of Humicola insolens cutinase in aqueous SDS. J Phys Chem 111:2941-2947
    • (2007) J Phys Chem , vol.111 , pp. 2941-2947
    • Nielsen, A.1    Borch, K.2    Westh, P.3
  • 35
    • 34249797596 scopus 로고    scopus 로고
    • Purification and characterization of mycobacterial phospholipase A: An activity associated with mycobacterial cutinase
    • 17416658 10.1128/JB.01909-06 1:CAS:528:DC%2BD2sXmt1eqtbc%3D
    • Parker SK, Curtin KM, Vasil ML (2007) Purification and characterization of mycobacterial phospholipase A: an activity associated with mycobacterial cutinase. J Bacteriol 189:4153-4160
    • (2007) J Bacteriol , vol.189 , pp. 4153-4160
    • Parker, S.K.1    Curtin, K.M.2    Vasil, M.L.3
  • 36
    • 34547548919 scopus 로고    scopus 로고
    • Optimizing the production of cutinase by Fusarium oxysporum using response surface methodology
    • 10.1016/j.enzmictec.2007.05.008 1:CAS:528:DC%2BD2sXosF2nt7Y%3D
    • Pio TF, Macedo GA (2007) Optimizing the production of cutinase by Fusarium oxysporum using response surface methodology. Enzyme Microb Technol 41:613-619
    • (2007) Enzyme Microb Technol , vol.41 , pp. 613-619
    • Pio, T.F.1    MacEdo, G.A.2
  • 37
    • 0038353703 scopus 로고    scopus 로고
    • Use of methylumbeliferyl-derivative substrates for lipase activity characterization
    • 10.1016/S1381-1177(03)00048-1 1:CAS:528:DC%2BD3sXltVSktL4%3D
    • Prim N, Sanchez M, Ruiz C, Pastor FI, Diaz P (2003) Use of methylumbeliferyl-derivative substrates for lipase activity characterization. J Mol Catal B Enzym 22:339-346
    • (2003) J Mol Catal B Enzym , vol.22 , pp. 339-346
    • Prim, N.1    Sanchez, M.2    Ruiz, C.3    Pastor, F.I.4    Diaz, P.5
  • 40
    • 45149110277 scopus 로고    scopus 로고
    • Optimization of the media ingredients for cutinase production from Colleotrichum lindemuthianum using mixture design experiments
    • 18331049 10.1021/bp070280n 1:CAS:528:DC%2BD1cXjtVaiu7w%3D
    • Rispoli F, Shah V (2008) Optimization of the media ingredients for cutinase production from Colleotrichum lindemuthianum using mixture design experiments. Biotechnol Prog 24:648-654
    • (2008) Biotechnol Prog , vol.24 , pp. 648-654
    • Rispoli, F.1    Shah, V.2
  • 41
    • 56749160103 scopus 로고    scopus 로고
    • Cloning and characterization of the Thcut1 gene encoding a cutinase of Trichoderma harzianum T34
    • 18987860 10.1007/s00294-008-0218-6 1:CAS:528:DC%2BD1cXhtlyhtrfJ
    • Rubio MB, Cardoza RE, Hermosa R, Gutierrez S, Monte E (2008) Cloning and characterization of the Thcut1 gene encoding a cutinase of Trichoderma harzianum T34. Curr Genet 54:301-312
    • (2008) Curr Genet , vol.54 , pp. 301-312
    • Rubio, M.B.1    Cardoza, R.E.2    Hermosa, R.3    Gutierrez, S.4    Monte, E.5
  • 42
    • 34447124589 scopus 로고    scopus 로고
    • Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5
    • 17505784 10.1007/s10529-007-9369-7 1:CAS:528:DC%2BD2sXnt1KitL8%3D
    • Sorensen JD, Petersen EI, Wiebe MG (2007) Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5. Biotechnol Lett 29:1227-1232
    • (2007) Biotechnol Lett , vol.29 , pp. 1227-1232
    • Sorensen, J.D.1    Petersen, E.I.2    Wiebe, M.G.3
  • 43
    • 80052266988 scopus 로고    scopus 로고
    • Effects of different solid state fermentation substrate on biochemical properties of cutinase from Fusarium sp
    • 10.1016/j.molcatb.2011.06.003 1:CAS:528:DC%2BC3MXhtV2ntbzF
    • Speranza P, de Oliveira Carvalho P, Macedo GA (2011) Effects of different solid state fermentation substrate on biochemical properties of cutinase from Fusarium sp. J Mol Catal B Enzym 72:181-186
    • (2011) J Mol Catal B Enzym , vol.72 , pp. 181-186
    • Speranza, P.1    De Oliveira Carvalho, P.2    MacEdo, G.A.3
  • 44
    • 84863172260 scopus 로고    scopus 로고
    • Isolation of a novel cutinase homolog with polyethylene terephthalate degrading activity from leaf-branch compost using a metagenomic approach
    • 10.1128/AEM.06725-11 1:CAS:528:DC%2BC38XjtVSntLY%3D
    • Sulaiman S, Yamato S, Kanaya E, Jaekim J, Koga Y, Takano K, Kanaya S (2012) Isolation of a novel cutinase homolog with polyethylene terephthalate degrading activity from leaf-branch compost using a metagenomic approach. Appl Environ Microb 78:1556-1562
    • (2012) Appl Environ Microb , vol.78 , pp. 1556-1562
    • Sulaiman, S.1    Yamato, S.2    Kanaya, E.3    Jaekim, J.4    Koga, Y.5    Takano, K.6    Kanaya, S.7
  • 45
    • 70449122484 scopus 로고    scopus 로고
    • Cloning and characterization of an intracellular esterase from the wine-associated lactic acid bacterium Oenococcus oeni
    • 19734337 10.1128/AEM.01563-09 1:CAS:528:DC%2BD1MXhsVGrsrbE
    • Sumby KM, Matthews AH, Grbin PR, Jiranek V (2009) Cloning and characterization of an intracellular esterase from the wine-associated lactic acid bacterium Oenococcus oeni. Appl Environ Microbiol 75:6729-6735
    • (2009) Appl Environ Microbiol , vol.75 , pp. 6729-6735
    • Sumby, K.M.1    Matthews, A.H.2    Grbin, P.R.3    Jiranek, V.4
  • 46
    • 84878474159 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119
    • Thumarat U, Nakamura R, Kawabata T, Suzuki H, Kawai F (2011) Biochemical and genetic analysis of cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119. Appl Microbiol Biotechnol 1:12
    • (2011) Appl Microbiol Biotechnol , vol.1 , pp. 12
    • Thumarat, U.1    Nakamura, R.2    Kawabata, T.3    Suzuki, H.4    Kawai, F.5
  • 47
    • 0015498958 scopus 로고
    • Determination of the structures of cutin monomers by a novel depolymerization procedure and combined gas chromatography
    • 5025631 10.1021/bi00760a025 1:CAS:528:DyaE38XktFKmtb8%3D
    • Walton TJ, Kolattukudy PE (1972) Determination of the structures of cutin monomers by a novel depolymerization procedure and combined gas chromatography. Biochemistry 11:1885-1897
    • (1972) Biochemistry , vol.11 , pp. 1885-1897
    • Walton, T.J.1    Kolattukudy, P.E.2
  • 48
    • 0036348909 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression of a redox-responsive cutinase from Monilinia fructicola (wint.) honey1
    • 11929215 10.1006/fgbi.2001.1320 1:CAS:528:DC%2BD38XisVOrsrY%3D
    • Wang GY, Michailides TJ, Hammock BD, Lee YM, Bostock RM (2002) Molecular cloning, characterization, and expression of a redox-responsive cutinase from Monilinia fructicola (wint.) honey1. 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


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