메뉴 건너뛰기




Volumn 34, Issue 4, 2015, Pages 243-255

Recent Advances in Fungal Hydrophobin Towards Using in Industry

Author keywords

Application; Hydrophobin; Industry; Legislation; Production; Purification

Indexed keywords

HYDROPHOBIN; NANOBUBBLE; CARBON DIOXIDE; DISULFIDE; FUNGAL PROTEIN; NANOMATERIAL; SURFACTANT;

EID: 84939263634     PISSN: 15723887     EISSN: 18758355     Source Type: Journal    
DOI: 10.1007/s10930-015-9621-2     Document Type: Review
Times cited : (49)

References (139)
  • 1
    • 77955845739 scopus 로고    scopus 로고
    • Biofoams and natural protein surfactants
    • COI: 1:CAS:528:DC%2BC3cXhtVKgsL%2FK
    • Cooper A, Kennedy MW (2010) Biofoams and natural protein surfactants. Biophys Chem 151:96–104
    • (2010) Biophys Chem , vol.151 , pp. 96-104
    • Cooper, A.1    Kennedy, M.W.2
  • 4
    • 84862296168 scopus 로고    scopus 로고
    • Hydrophobins: exceptional proteins for many applications in brewery environment and other bio-industries
    • COI: 1:CAS:528:DC%2BC38Xht1alsL%2FF
    • Khalesi M, Deckers SM, Gebreurs K, Vissers L, Verachtert H, Derdenlickx G (2012) Hydrophobins: exceptional proteins for many applications in brewery environment and other bio-industries. Cerevisia 37:3–9
    • (2012) Cerevisia , vol.37 , pp. 3-9
    • Khalesi, M.1    Deckers, S.M.2    Gebreurs, K.3    Vissers, L.4    Verachtert, H.5    Derdenlickx, G.6
  • 6
    • 68949184106 scopus 로고    scopus 로고
    • Industrial performance proteins: hydrophobin-learning from nature
    • Subkowski T, Karos M, Subkowski T (2007) Industrial performance proteins: hydrophobin-learning from nature. J Biotechnol 131:212–213
    • (2007) J Biotechnol , vol.131 , pp. 212-213
    • Subkowski, T.1    Karos, M.2    Subkowski, T.3
  • 7
    • 0036193136 scopus 로고    scopus 로고
    • Identification of a hydrophobin gene that is developmentally regulated in the Ectomycorrhizal fungus Tricholoma terreum
    • COI: 1:CAS:528:DC%2BD38XitFSjsLY%3D
    • Mankel A, Krause K, Kothe E (2002) Identification of a hydrophobin gene that is developmentally regulated in the Ectomycorrhizal fungus Tricholoma terreum. Appl Environ Microb 68:1408–1413
    • (2002) Appl Environ Microb , vol.68 , pp. 1408-1413
    • Mankel, A.1    Krause, K.2    Kothe, E.3
  • 8
    • 80052088938 scopus 로고    scopus 로고
    • Amphiphilic nanotubes in the crystal structure of a biosurfactant protein hydrophobin HFBII
    • COI: 1:CAS:528:DC%2BC3MXhtVOjsrzM
    • Kallio JM, Rouvinen J (2011) Amphiphilic nanotubes in the crystal structure of a biosurfactant protein hydrophobin HFBII. Chem Commun 47:9843–9845
    • (2011) Chem Commun , vol.47 , pp. 9843-9845
    • Kallio, J.M.1    Rouvinen, J.2
  • 9
    • 84883317541 scopus 로고    scopus 로고
    • The RodA Hydrophobin on Aspergillus masks Dectin-1- and Dectin-2-dependent responses and enhances fungal survival in vivo
    • COI: 1:CAS:528:DC%2BC3sXhtlSgtb%2FK
    • Carrion S-J, Leal SM Jr, Ghannoum MA, Aimanianda V, Latge J-P, Pearlman E (2013) The RodA Hydrophobin on Aspergillus masks Dectin-1- and Dectin-2-dependent responses and enhances fungal survival in vivo. J Immunol 191:2581–2588
    • (2013) J Immunol , vol.191 , pp. 2581-2588
    • Carrion, S.-J.1    Leal, S.M.2    Ghannoum, M.A.3    Aimanianda, V.4    Latge, J.-P.5    Pearlman, E.6
  • 10
    • 0034775004 scopus 로고    scopus 로고
    • Hydrophobins: multipurpose proteins
    • Wösten HAB (2001) Hydrophobins: multipurpose proteins. Annu Rev Microbiol 55:625–646
    • (2001) Annu Rev Microbiol , vol.55 , pp. 625-646
    • Wösten, H.A.B.1
  • 11
    • 68949194700 scopus 로고    scopus 로고
    • Hydrophobins: proteins that self assemble at interfaces
    • COI: 1:CAS:528:DC%2BD1MXhtVegsbzM
    • Linder MB (2009) Hydrophobins: proteins that self assemble at interfaces. Curr Opin Colloid Interface Sci 14:356–363
    • (2009) Curr Opin Colloid Interface Sci , vol.14 , pp. 356-363
    • Linder, M.B.1
  • 12
    • 0001436806 scopus 로고    scopus 로고
    • Hydrophobins, from molecular structure to multiple functions in fungal development
    • Wösten HAB, Wessels JGH (1997) Hydrophobins, from molecular structure to multiple functions in fungal development. Mycoscience 38:363–374
    • (1997) Mycoscience , vol.38 , pp. 363-374
    • Wösten, H.A.B.1    Wessels, J.G.H.2
  • 13
    • 0030886123 scopus 로고    scopus 로고
    • Differential expression of the vegetative and spore bound hydrophobins of Trichoderma reesei cloning and characterization of hfb2 gene
    • Nakari-Setälä T, Aro N, Ilmén M, Muñoz G, Kalkinnen N, Penttilä M (1997) Differential expression of the vegetative and spore bound hydrophobins of Trichoderma reesei cloning and characterization of hfb2 gene. Eur J Biochem 248:415–423
    • (1997) Eur J Biochem , vol.248 , pp. 415-423
    • Nakari-Setälä, T.1    Aro, N.2    Ilmén, M.3    Muñoz, G.4    Kalkinnen, N.5    Penttilä, M.6
  • 15
    • 23444457742 scopus 로고    scopus 로고
    • Hydrophobins: proteins with potential
    • COI: 1:CAS:528:DC%2BD2MXntVCqtb0%3D
    • Hektor HJ, Scholtmeijer K (2005) Hydrophobins: proteins with potential. Curr Opin Biotech 16:434–439
    • (2005) Curr Opin Biotech , vol.16 , pp. 434-439
    • Hektor, H.J.1    Scholtmeijer, K.2
  • 17
    • 37749006898 scopus 로고    scopus 로고
    • Interactions of hydrophobin proteins in solution studied by small-angle X-ray scattering
    • COI: 1:CAS:528:DC%2BD1cXkvFA%3D
    • Kisko K, Szilvay GR, Vainio U, Linder MB, Serimaa R (2008) Interactions of hydrophobin proteins in solution studied by small-angle X-ray scattering. Biophys J 94:198–206
    • (2008) Biophys J , vol.94 , pp. 198-206
    • Kisko, K.1    Szilvay, G.R.2    Vainio, U.3    Linder, M.B.4    Serimaa, R.5
  • 18
    • 33646363317 scopus 로고    scopus 로고
    • Interaction and comparison of a Class I hydrophobin from Schizophyllum commune and Class II hydrophobins from Trichoderma reesei
    • COI: 1:CAS:528:DC%2BD28XisFemtr4%3D
    • Askolin S, Linder M, Scholtmeijer K, Tenkanen M, Penttilä M, de Vocht ML, Wösten HAB (2006) Interaction and comparison of a Class I hydrophobin from Schizophyllumcommune and Class II hydrophobins from Trichoderma reesei. Biomacromolecules 7:1295–1301
    • (2006) Biomacromolecules , vol.7 , pp. 1295-1301
    • Askolin, S.1    Linder, M.2    Scholtmeijer, K.3    Tenkanen, M.4    Penttilä, M.5    de Vocht, M.L.6    Wösten, H.A.B.7
  • 20
    • 84878239596 scopus 로고    scopus 로고
    • Surface pressure and elasticity of hydrophobin HFBII layers on the air–water interface: rheology versus structure detected by AFM imaging
    • COI: 1:CAS:528:DC%2BC3sXmtleksLg%3D
    • Stanimirova RD, Gurkov TD, Kralchevsky PA, Balashev KT, Stoyanov SD, Pelan EG (2013) Surface pressure and elasticity of hydrophobin HFBII layers on the air–water interface: rheology versus structure detected by AFM imaging. Langmuir 29:6053–6067
    • (2013) Langmuir , vol.29 , pp. 6053-6067
    • Stanimirova, R.D.1    Gurkov, T.D.2    Kralchevsky, P.A.3    Balashev, K.T.4    Stoyanov, S.D.5    Pelan, E.G.6
  • 21
    • 0028045183 scopus 로고
    • Developmental regulation of fungal cell wall formation
    • COI: 1:CAS:528:DyaK2cXmtVSntbY%3D
    • Wessels JGH (1994) Developmental regulation of fungal cell wall formation. Annu Rev Phytopathol 32:413–437
    • (1994) Annu Rev Phytopathol , vol.32 , pp. 413-437
    • Wessels, J.G.H.1
  • 22
    • 0025875745 scopus 로고
    • Rodletless, a new Aspergillus developmental mutant induced by directed gene inactivation
    • COI: 1:CAS:528:DyaK38XhtVSgu7s%3D
    • Stringer MA, Dean RA, Sewall TC, Timberlake WE (1991) Rodletless, a new Aspergillus developmental mutant induced by directed gene inactivation. Gene Dev 5:1161–1171
    • (1991) Gene Dev , vol.5 , pp. 1161-1171
    • Stringer, M.A.1    Dean, R.A.2    Sewall, T.C.3    Timberlake, W.E.4
  • 23
    • 0034888635 scopus 로고    scopus 로고
    • The hydrophobins HFBI and HFBII from Trichoderma reesei showing efficient interactions with nonionic surfactants in aqueous two-phase systems
    • COI: 1:CAS:528:DC%2BD3MXjsFSqt74%3D
    • Linder M, Selber K, Nakari-Setälä T, Qiao M, Kula M-R, Penttilä M (2001) The hydrophobins HFBI and HFBII from Trichoderma reesei showing efficient interactions with nonionic surfactants in aqueous two-phase systems. Biomacromolecules 2:511–517
    • (2001) Biomacromolecules , vol.2 , pp. 511-517
    • Linder, M.1    Selber, K.2    Nakari-Setälä, T.3    Qiao, M.4    Kula, M.-R.5    Penttilä, M.6
  • 25
    • 27944509148 scopus 로고    scopus 로고
    • The Trichoderma reesei hydrophobin genes hfb1 and hfb2 have diversal functions in fungal development
    • COI: 1:CAS:528:DC%2BD2MXht1Gns73I
    • Askolin S, Penttilä M, Wösten HAB, Nakari-Setälä T (2005) The Trichoderma reesei hydrophobin genes hfb1 and hfb2 have diversal functions in fungal development. FEMS Microbiol Lett 253:281–288
    • (2005) FEMS Microbiol Lett , vol.253 , pp. 281-288
    • Askolin, S.1    Penttilä, M.2    Wösten, H.A.B.3    Nakari-Setälä, T.4
  • 27
    • 33748937555 scopus 로고    scopus 로고
    • The surprising complexity of signal sequences
    • COI: 1:CAS:528:DC%2BD28XhtVagtrrI
    • Hegde RS, Bernstein HD (2006) The surprising complexity of signal sequences. Trends Biochem Sci 31:563–571
    • (2006) Trends Biochem Sci , vol.31 , pp. 563-571
    • Hegde, R.S.1    Bernstein, H.D.2
  • 28
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP, and related tools
    • COI: 1:CAS:528:DC%2BD2sXhtFGnur%2FF
    • Emanuelsson O, Brunak S, von Heijne G, Nielsen H (2007) Locating proteins in the cell using TargetP, SignalP, and related tools. Nat Protoc 2:953–971
    • (2007) Nat Protoc , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 30
    • 34249659125 scopus 로고    scopus 로고
    • The relation between solution association and surface activity of the hydrophobin HFBI from Trichoderma reseei
    • COI: 1:CAS:528:DC%2BD2sXmtFOiu7w%3D
    • Szilvay GR, Kisko K, Serimaa R, Linder MB (2007) The relation between solution association and surface activity of the hydrophobin HFBI from Trichoderma reseei. FEBS Lett 581:2721–2726
    • (2007) FEBS Lett , vol.581 , pp. 2721-2726
    • Szilvay, G.R.1    Kisko, K.2    Serimaa, R.3    Linder, M.B.4
  • 31
    • 34547355208 scopus 로고    scopus 로고
    • Surface properties of class II hydrophobins from Trichoderma reesei and influence on bubble stability
    • COI: 1:CAS:528:DC%2BD2sXms1Wrt74%3D
    • Cox AR, Cagnolm F, Russell AB, Izzard MJ (2007) Surface properties of class II hydrophobins from Trichoderma reesei and influence on bubble stability. Langmuir 23:7995–8002
    • (2007) Langmuir , vol.23 , pp. 7995-8002
    • Cox, A.R.1    Cagnolm, F.2    Russell, A.B.3    Izzard, M.J.4
  • 32
    • 78649609527 scopus 로고
    • Das Ueberschäumen (Wildwerden) des Bieres
    • COI: 1:CAS:528:DyaA1cXlslKlsA%3D%3D
    • Helm E, Richardt OC (1938) Das Ueberschäumen (Wildwerden) des Bieres. Wochenschrift für Brauerei 55(12):89–94
    • (1938) Wochenschrift für Brauerei , vol.55 , Issue.12 , pp. 89-94
    • Helm, E.1    Richardt, O.C.2
  • 33
    • 84978598014 scopus 로고
    • The mechanism of gushing—a review
    • COI: 1:CAS:528:DyaE3sXkvFSntb4%3D
    • Gardner RJ (1973) The mechanism of gushing—a review. J Inst Brewing 79:275–283
    • (1973) J Inst Brewing , vol.79 , pp. 275-283
    • Gardner, R.J.1
  • 35
    • 84859121890 scopus 로고    scopus 로고
    • Identification and characterization of gushing-active hydrophobins from Fusarium graminearum and related species
    • COI: 1:CAS:528:DC%2BC38Xks1Olsb0%3D
    • Sarlin T, Kivioja T, Kalkkinen N, Linder MB, Nakari-Setälä T (2012) Identification and characterization of gushing-active hydrophobins from Fusarium graminearum and related species. J Basic Microb 52:184–194
    • (2012) J Basic Microb , vol.52 , pp. 184-194
    • Sarlin, T.1    Kivioja, T.2    Kalkkinen, N.3    Linder, M.B.4    Nakari-Setälä, T.5
  • 36
    • 84865363402 scopus 로고    scopus 로고
    • Sparkling wines: features and trends from tradition
    • COI: 1:CAS:528:DC%2BC38XhslKhtbvJ
    • Buxaderas S, Lopez-Tamames E (2012) Sparkling wines: features and trends from tradition. Adv Food Nutr Res 66:1–45
    • (2012) Adv Food Nutr Res , vol.66 , pp. 1-45
    • Buxaderas, S.1    Lopez-Tamames, E.2
  • 37
    • 79952504712 scopus 로고    scopus 로고
    • Induction of gushing with recombinant Class II hydrophobin FcHyd5p from Fusarium culmorum and the impact of hop compounds on its gushing potential
    • COI: 1:CAS:528:DC%2BC3MXmtVKhtbw%3D
    • Lutterschmid G, Stübner M, Vogel RF, Niessen L (2010) Induction of gushing with recombinant Class II hydrophobin FcHyd5p from Fusarium culmorum and the impact of hop compounds on its gushing potential. J Inst Brewing 116:339–347
    • (2010) J Inst Brewing , vol.116 , pp. 339-347
    • Lutterschmid, G.1    Stübner, M.2    Vogel, R.F.3    Niessen, L.4
  • 39
    • 18444400868 scopus 로고    scopus 로고
    • Effects of three Fusarium species on the quality of barley and malt
    • COI: 1:CAS:528:DC%2BD2MXjvFSktbs%3D
    • Sarlin T, Laitila A, Pekkarinen A, Haikara A (2005) Effects of three Fusarium species on the quality of barley and malt. J Am Soc Brew Chem 63:43–49
    • (2005) J Am Soc Brew Chem , vol.63 , pp. 43-49
    • Sarlin, T.1    Laitila, A.2    Pekkarinen, A.3    Haikara, A.4
  • 40
    • 0036370568 scopus 로고    scopus 로고
    • Hippeli S, Elstner EF (2002) Are hydrophobins and/or non-specific lipid transfer proteins responsible for gushing in beer? New hypotheses on the chemical nature of gushing inducing factors. Verlag der Zeitschrift für Naturforschung, Tübingen , 1–7
    • Hippeli S, Elstner EF (2002) Are hydrophobins and/or non-specific lipid transfer proteins responsible for gushing in beer? New hypotheses on the chemical nature of gushing inducing factors. Verlag der Zeitschrift für Naturforschung, Tübingen www.znaturforsch.com, 1–7
  • 41
    • 27444436304 scopus 로고    scopus 로고
    • Fungal hydrophobins as predictors of the gushing activity of malt
    • COI: 1:CAS:528:DC%2BD2MXhtFGrsLrM
    • Sarlin T, Nakari-Setälä T, Linder M, Penttilä M, Haikara A (2005) Fungal hydrophobins as predictors of the gushing activity of malt. J Inst Brewing 111:105–111
    • (2005) J Inst Brewing , vol.111 , pp. 105-111
    • Sarlin, T.1    Nakari-Setälä, T.2    Linder, M.3    Penttilä, M.4    Haikara, A.5
  • 42
    • 84939285155 scopus 로고    scopus 로고
    • Interaction of class II hydrophobins with hydrophobic interfaces as a basis for solving primary gushing problems in the brewing industry
    • KU Leuven, Belgium
    • Shokribousjein Z (2014) Interaction of class II hydrophobins with hydrophobic interfaces as a basis for solving primary gushing problems in the brewing industry. Dissertation, KU Leuven, Belgium
    • (2014) Dissertation
    • Shokribousjein, Z.1
  • 43
    • 78649557606 scopus 로고    scopus 로고
    • Combined particle analysis as a new tool to predict gushing shown with alcohol-free beverage products
    • COI: 1:CAS:528:DC%2BC3cXhtlaktLfE
    • Christian M, Titze T, Ilberg V, Jacob F (2010) Combined particle analysis as a new tool to predict gushing shown with alcohol-free beverage products. BrewingScience 63:72–79
    • (2010) BrewingScience , vol.63 , pp. 72-79
    • Christian, M.1    Titze, T.2    Ilberg, V.3    Jacob, F.4
  • 44
    • 80755126764 scopus 로고    scopus 로고
    • Novel perspectives in gushing analysis: a review
    • COI: 1:CAS:528:DC%2BC38XhtlKms7s%3D
    • Christian M, Titze J, Ilberg V, Jacob F (2011) Novel perspectives in gushing analysis: a review. J Inst Brewing 117:295–313
    • (2011) J Inst Brewing , vol.117 , pp. 295-313
    • Christian, M.1    Titze, J.2    Ilberg, V.3    Jacob, F.4
  • 50
    • 0036247045 scopus 로고    scopus 로고
    • Process technological effects of deletion and amplification of hydrophobins I and II in transformants of Trichoderma reesei
    • COI: 1:CAS:528:DC%2BD38XktFCqtb0%3D
    • Bailey MJ, Askolin S, Hörhammer N, Tenkanen M, Linder M, Penttilä M, Nakari-Setälä T (2002) Process technological effects of deletion and amplification of hydrophobins I and II in transformants of Trichoderma reesei. Appl Microbiol Biot 58:721–727
    • (2002) Appl Microbiol Biot , vol.58 , pp. 721-727
    • Bailey, M.J.1    Askolin, S.2    Hörhammer, N.3    Tenkanen, M.4    Linder, M.5    Penttilä, M.6    Nakari-Setälä, T.7
  • 51
    • 0034789486 scopus 로고    scopus 로고
    • Overproduction, purification and characterization of the Trichoderma reesei hydrophobin HFBI
    • COI: 1:CAS:528:DC%2BD3MXotVSnu7c%3D
    • Askolin S, Nakari-Setälä T, Tenkanen M (2001) Overproduction, purification and characterization of the Trichoderma reesei hydrophobin HFBI. Appl Microbiol Biot 57:124–130
    • (2001) Appl Microbiol Biot , vol.57 , pp. 124-130
    • Askolin, S.1    Nakari-Setälä, T.2    Tenkanen, M.3
  • 52
    • 26944499474 scopus 로고    scopus 로고
    • Adsorption of hydrophobin proteins at hydrophobic and hydrophilic interfaces
    • COI: 1:CAS:528:DC%2BD2MXns1Wiurg%3D
    • Lumsdon SO, Green J, Stieglitz B (2005) Adsorption of hydrophobin proteins at hydrophobic and hydrophilic interfaces. Colloid Surf B 44(4):172–178
    • (2005) Colloid Surf B , vol.44 , Issue.4 , pp. 172-178
    • Lumsdon, S.O.1    Green, J.2    Stieglitz, B.3
  • 53
    • 51049104790 scopus 로고    scopus 로고
    • Exceptional stability of food foams using class II hydrophobin HFBII
    • COI: 1:CAS:528:DC%2BD1cXhtFSqsrrN
    • Cox AR, Aldred DL, Russell AB (2009) Exceptional stability of food foams using class II hydrophobin HFBII. Food Hydrocolloid 23:366–376
    • (2009) Food Hydrocolloid , vol.23 , pp. 366-376
    • Cox, A.R.1    Aldred, D.L.2    Russell, A.B.3
  • 54
    • 77950822737 scopus 로고    scopus 로고
    • On the link between foam coarsening and surface rheology: why hydrophobins are so different
    • COI: 1:CAS:528:DC%2BC3cXksVGht7Y%3D
    • Blijdenstein TBJ, de Groot PWN, Stoyanov SD (2010) On the link between foam coarsening and surface rheology: why hydrophobins are so different. Soft Matter 6:1799–1808
    • (2010) Soft Matter , vol.6 , pp. 1799-1808
    • Blijdenstein, T.B.J.1    de Groot, P.W.N.2    Stoyanov, S.D.3
  • 55
    • 79951671768 scopus 로고    scopus 로고
    • Expression and purification of a functionally active class I fungal hydrophobin from the entomopathogenic fungus Beauveria bassiana in E. coli
    • COI: 1:CAS:528:DC%2BC3MXovVSmsQ%3D%3D
    • Kirkland BH, Keyhani NO (2011) Expression and purification of a functionally active class I fungal hydrophobin from the entomopathogenic fungus Beauveria bassiana in E. coli. J Ind Microbial Biot 38:327–335
    • (2011) J Ind Microbial Biot , vol.38 , pp. 327-335
    • Kirkland, B.H.1    Keyhani, N.O.2
  • 56
    • 79952818697 scopus 로고    scopus 로고
    • Integrated recirculating foam fractionation for the continuous recovery of biosurfactant from fermenters
    • COI: 1:CAS:528:DC%2BC3MXjvVenur4%3D
    • Winterburn JB, Russell AB, Martin PJ (2011) Integrated recirculating foam fractionation for the continuous recovery of biosurfactant from fermenters. Biochem Eng J 54:132–139
    • (2011) Biochem Eng J , vol.54 , pp. 132-139
    • Winterburn, J.B.1    Russell, A.B.2    Martin, P.J.3
  • 57
    • 84895069501 scopus 로고    scopus 로고
    • High-energy X-ray tomography analysis of a metal packing biofilm reactor for the production of lipopeptides by Bacillus subtilis
    • COI: 1:CAS:528:DC%2BC3sXhtVShtL7F
    • Zune Q, Soyeurt D, Toye D, Ongena M, Thonart P, Delvigne F (2014) High-energy X-ray tomography analysis of a metal packing biofilm reactor for the production of lipopeptides by Bacillus subtilis. J Chem Technol Biotechnol 89:382–390
    • (2014) J Chem Technol Biotechnol , vol.89 , pp. 382-390
    • Zune, Q.1    Soyeurt, D.2    Toye, D.3    Ongena, M.4    Thonart, P.5    Delvigne, F.6
  • 58
    • 33749402654 scopus 로고    scopus 로고
    • Optimization of protein recovery by foam separation using response surface methodology
    • COI: 1:CAS:528:DC%2BD2sXit1Gitrc%3D
    • Aksay S, Mazza G (2007) Optimization of protein recovery by foam separation using response surface methodology. J Food Eng 79:598–606
    • (2007) J Food Eng , vol.79 , pp. 598-606
    • Aksay, S.1    Mazza, G.2
  • 59
    • 33846115013 scopus 로고    scopus 로고
    • Batch foam separation of a soluble protein
    • COI: 1:CAS:528:DC%2BD2sXktlKnsA%3D%3D
    • Maruyama H, Seki H, Suzuki A, Inoue N (2007) Batch foam separation of a soluble protein. Water Res 41:710–718
    • (2007) Water Res , vol.41 , pp. 710-718
    • Maruyama, H.1    Seki, H.2    Suzuki, A.3    Inoue, N.4
  • 60
    • 33749590377 scopus 로고    scopus 로고
    • Towards commercial production of microbial surfactants
    • COI: 1:CAS:528:DC%2BD28XhtVOrt77J
    • Mukherjee S, Das P, Sen R (2006) Towards commercial production of microbial surfactants. Trends Biotechnol 24:509–515
    • (2006) Trends Biotechnol , vol.24 , pp. 509-515
    • Mukherjee, S.1    Das, P.2    Sen, R.3
  • 61
    • 32944465970 scopus 로고    scopus 로고
    • Rheology and convective heat transfer of colloidal gas aphrons in horizontal mini-channels
    • Tseng H, Pilon L, Gopinath R, Warrier GR (2006) Rheology and convective heat transfer of colloidal gas aphrons in horizontal mini-channels. Int J Heat Fluid Fl 27:298–310
    • (2006) Int J Heat Fluid Fl , vol.27 , pp. 298-310
    • Tseng, H.1    Pilon, L.2    Gopinath, R.3    Warrier, G.R.4
  • 63
    • 35348966768 scopus 로고    scopus 로고
    • Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer films
    • COI: 1:CAS:528:DC%2BD2sXhtVOmtbrO
    • Kallio JM, Linder MB, Rouvinen J (2007) Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer films. J Biol Chem 282:28733–28739
    • (2007) J Biol Chem , vol.282 , pp. 28733-28739
    • Kallio, J.M.1    Linder, M.B.2    Rouvinen, J.3
  • 64
    • 33847721475 scopus 로고    scopus 로고
    • Self-assembled hydrophobin protein films at the air–water interface: structural analysis and molecular engineering
    • COI: 1:CAS:528:DC%2BD2sXhsFOktrg%3D
    • Szilvay GR, Paananen A, Laurikainen K, Vuorimaa E, Lemmetyinen H, Peltonen J, Linder MB (2007) Self-assembled hydrophobin protein films at the air–water interface: structural analysis and molecular engineering. Biochemistry 46:2345–2354
    • (2007) Biochemistry , vol.46 , pp. 2345-2354
    • Szilvay, G.R.1    Paananen, A.2    Laurikainen, K.3    Vuorimaa, E.4    Lemmetyinen, H.5    Peltonen, J.6    Linder, M.B.7
  • 65
    • 75949109975 scopus 로고    scopus 로고
    • Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana
    • COI: 1:CAS:528:DC%2BC3cXmsFegtrs%3D
    • Joensuu JJ, Conley AJ, Lienemann M, Brandle JE, Linder MB, Menassa R (2010) Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana. Plant Physiol 152:622–633
    • (2010) Plant Physiol , vol.152 , pp. 622-633
    • Joensuu, J.J.1    Conley, A.J.2    Lienemann, M.3    Brandle, J.E.4    Linder, M.B.5    Menassa, R.6
  • 67
    • 0032426559 scopus 로고    scopus 로고
    • Retention in reversed-phase chromatography: partition or adsorption?
    • COI: 1:CAS:528:DyaK1MXnvFGksg%3D%3D
    • Vailaya A, Horvath C (1998) Retention in reversed-phase chromatography: partition or adsorption? J Chromatogr A 829:1–27
    • (1998) J Chromatogr A , vol.829 , pp. 1-27
    • Vailaya, A.1    Horvath, C.2
  • 69
    • 0028597937 scopus 로고
    • Interfacial self-assembly of a hydrophobin into an amphipathic protein membrane mediates fungal attachment to hydrophobic surfaces
    • Wösten HAB, Schuren FHJ, Wessels JGH (1994) Interfacial self-assembly of a hydrophobin into an amphipathic protein membrane mediates fungal attachment to hydrophobic surfaces. EMBO J 13:5848–5854
    • (1994) EMBO J , vol.13 , pp. 5848-5854
    • Wösten, H.A.B.1    Schuren, F.H.J.2    Wessels, J.G.H.3
  • 70
    • 34247387198 scopus 로고    scopus 로고
    • Bioactive surface modification of mica and poly(dimethylsiloxane) with hydrophobins for protein immobilization
    • COI: 1:CAS:528:DC%2BD2sXisVOmtbk%3D
    • Qin M, Wang L-K, Feng X-Z (2007) Bioactive surface modification of mica and poly(dimethylsiloxane) with hydrophobins for protein immobilization. Langmuir 23:4465–4471
    • (2007) Langmuir , vol.23 , pp. 4465-4471
    • Qin, M.1    Wang, L.-K.2    Feng, X.-Z.3
  • 72
    • 0034911485 scopus 로고    scopus 로고
    • Fungal hydrophobins in medical and technical applications
    • COI: 1:CAS:528:DC%2BD3MXls1Shtrw%3D
    • Scholtmeijer K, Wessels JGH, Wösten HAB (2001) Fungal hydrophobins in medical and technical applications. Appl Microbiol Biot 56:1–8
    • (2001) Appl Microbiol Biot , vol.56 , pp. 1-8
    • Scholtmeijer, K.1    Wessels, J.G.H.2    Wösten, H.A.B.3
  • 73
    • 4444342809 scopus 로고    scopus 로고
    • Probing the self-assembly and the accompanying structural changes of hydrophobin SC3 on a hydrophobic surface by mass spectrometry
    • COI: 1:CAS:528:DC%2BD2cXns1SksLk%3D
    • Wang X, Permentier HP, Rink R, Kruijtzer JAW, Liskamp RMJ, Wösten HAB, Poolman B, Robillard GT (2004) Probing the self-assembly and the accompanying structural changes of hydrophobin SC3 on a hydrophobic surface by mass spectrometry. Biophysical J 87:1919–1928
    • (2004) Biophysical J , vol.87 , pp. 1919-1928
    • Wang, X.1    Permentier, H.P.2    Rink, R.3    Kruijtzer, J.A.W.4    Liskamp, R.M.J.5    Wösten, H.A.B.6    Poolman, B.7    Robillard, G.T.8
  • 75
    • 34548822143 scopus 로고    scopus 로고
    • Stabilization of bubbles and foams
    • COI: 1:CAS:528:DC%2BD2sXhtFSitr%2FN
    • Murray BS (2007) Stabilization of bubbles and foams. Curr Opin Colloid Interface Sci 12:232–241
    • (2007) Curr Opin Colloid Interface Sci , vol.12 , pp. 232-241
    • Murray, B.S.1
  • 76
    • 77950567158 scopus 로고    scopus 로고
    • Recombinantly produced hydrophobins from fungal analogues as highly surface-active performance proteins
    • COI: 1:CAS:528:DC%2BC3cXhtFOju7Y%3D
    • Wohlleben W, Subkowski T, Bollschweiler C, von Vacano B, Liu Y, Schrepp W, Baus U (2010) Recombinantly produced hydrophobins from fungal analogues as highly surface-active performance proteins. Euro Biophys J 39:457–468
    • (2010) Euro Biophys J , vol.39 , pp. 457-468
    • Wohlleben, W.1    Subkowski, T.2    Bollschweiler, C.3    von Vacano, B.4    Liu, Y.5    Schrepp, W.6    Baus, U.7
  • 77
    • 67349263876 scopus 로고    scopus 로고
    • Hydrophobins stabilised air-filled emulsions for the food industry
    • COI: 1:CAS:528:DC%2BD1MXmsFKmtrw%3D
    • Tchuenbou-Magaia FL, Norton IT, Cox PW (2009) Hydrophobins stabilised air-filled emulsions for the food industry. Food Hydrocolloid 23:1877–1885
    • (2009) Food Hydrocolloid , vol.23 , pp. 1877-1885
    • Tchuenbou-Magaia, F.L.1    Norton, I.T.2    Cox, P.W.3
  • 80
    • 4644247411 scopus 로고    scopus 로고
    • Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase systems
    • COI: 1:CAS:528:DC%2BD2cXmvFChsbc%3D
    • Linder MB, Qiao M, Laumen F, Selber K, Hyytia T, Nakari-Setälä T, Penttilä ME (2004) Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase systems. Biochemistry 43:11873–11882
    • (2004) Biochemistry , vol.43 , pp. 11873-11882
    • Linder, M.B.1    Qiao, M.2    Laumen, F.3    Selber, K.4    Hyytia, T.5    Nakari-Setälä, T.6    Penttilä, M.E.7
  • 81
    • 15444373003 scopus 로고    scopus 로고
    • Preparing catalytic surfaces for sensing applications by immobilizing enzymes via hydrophobin layers
    • COI: 1:CAS:528:DC%2BD2MXhtlCgs7k%3D
    • Corvis Y, Walcarius A, Rink R, Mrabet NT, Rogalska E (2005) Preparing catalytic surfaces for sensing applications by immobilizing enzymes via hydrophobin layers. Anal Chem 77:1622–1630
    • (2005) Anal Chem , vol.77 , pp. 1622-1630
    • Corvis, Y.1    Walcarius, A.2    Rink, R.3    Mrabet, N.T.4    Rogalska, E.5
  • 82
    • 33744521389 scopus 로고    scopus 로고
    • Nanoscale reduction in surface friction of polymer surfaces modified with SC3 hydrophobin from Schizophyllum commune
    • COI: 1:CAS:528:DC%2BD28Xjt1WlsL0%3D
    • Misra R, Li J, Cannon GC, Morgan SE (2006) Nanoscale reduction in surface friction of polymer surfaces modified with SC3 hydrophobin from Schizophyllum commune. Biomacromolecules 7:1463–1470
    • (2006) Biomacromolecules , vol.7 , pp. 1463-1470
    • Misra, R.1    Li, J.2    Cannon, G.C.3    Morgan, S.E.4
  • 83
    • 35649017604 scopus 로고    scopus 로고
    • Two methods for glass surface modification and their application in protein immobilization
    • COI: 1:CAS:528:DC%2BD2sXht12hsLnO
    • Qin M, Hou S, Wang L, Feng X, Wang R, Yang Y, Wang C, Yu L, Shao B, Qiao M (2007) Two methods for glass surface modification and their application in protein immobilization. Colloid Surf B 60:243–249
    • (2007) Colloid Surf B , vol.60 , pp. 243-249
    • Qin, M.1    Hou, S.2    Wang, L.3    Feng, X.4    Wang, R.5    Yang, Y.6    Wang, C.7    Yu, L.8    Shao, B.9    Qiao, M.10
  • 84
    • 40849124046 scopus 로고    scopus 로고
    • Hydrophobin (HFBI): a potential fusion partner for one-step purification of recombinant proteins from insect cells
    • COI: 1:CAS:528:DC%2BD1cXjs1SlsLg%3D
    • Lahtinen T, Linder MB, Nakari-Setälä T, Oker-Blom C (2008) Hydrophobin (HFBI): a potential fusion partner for one-step purification of recombinant proteins from insect cells. Protein Express Purif 59:18–24
    • (2008) Protein Express Purif , vol.59 , pp. 18-24
    • Lahtinen, T.1    Linder, M.B.2    Nakari-Setälä, T.3    Oker-Blom, C.4
  • 86
    • 77957339506 scopus 로고    scopus 로고
    • Noncovalently functionalized multi-wall carbon nanotubes in aqueous solution using the hydrophobin HFBI and their electroanalytical application
    • COI: 1:CAS:528:DC%2BC3cXht1Onu73N
    • Wang X, Wang H, Huang Y, Zhao Z, Qin X, Wang Y, Miao Z, Chena Q, Qiao M (2010) Noncovalently functionalized multi-wall carbon nanotubes in aqueous solution using the hydrophobin HFBI and their electroanalytical application. Biosens Bioelectron 26:1104–1108
    • (2010) Biosens Bioelectron , vol.26 , pp. 1104-1108
    • Wang, X.1    Wang, H.2    Huang, Y.3    Zhao, Z.4    Qin, X.5    Wang, Y.6    Miao, Z.7    Chena, Q.8    Qiao, M.9
  • 87
    • 84973387886 scopus 로고    scopus 로고
    • Method for coating an object with hydrophobin at low temperatures
    • Rink R, Scholtmeijer K (2005) Method for coating an object with hydrophobin at low temperatures. Patent WO 2005068087 A2
    • (2005) Patent WO , pp. A2
    • Rink, R.1    Scholtmeijer, K.2
  • 89
    • 84973303099 scopus 로고    scopus 로고
    • Method for coating an object with hydrophobin at low temperatures
    • Rink R, Scholtmeijer K (2007) Method for coating an object with hydrophobin at low temperatures. Patent US 20070166346 A1
    • (2007) Patent US , pp. A1
    • Rink, R.1    Scholtmeijer, K.2
  • 91
    • 84973355777 scopus 로고    scopus 로고
    • Thermophilic hydrophobin proteins and applications for surface modification
    • Sweigard JA, Stieglitz B (2009) Thermophilic hydrophobin proteins and applications for surface modification. Patent US 7476537 B2
    • (2009) Patent US , pp. B2
    • Sweigard, J.A.1    Stieglitz, B.2
  • 96
    • 84973346604 scopus 로고    scopus 로고
    • Hydrophobin composition and process for treating surfaces
    • Li F, You Z, Rishton V (2015) Hydrophobin composition and process for treating surfaces. Patent WO 2015051121 A1
    • (2015) Patent WO , pp. A1
    • Li, F.1    You, Z.2    Rishton, V.3
  • 98
    • 0036708010 scopus 로고    scopus 로고
    • Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei
    • COI: 1:CAS:528:DC%2BD38XmslCisro%3D
    • Linder M, Szilvay GR, Nakari-Setälä T, Soderlund H, Penttilä M (2002) Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei. Protein Sci 11:2257–2266
    • (2002) Protein Sci , vol.11 , pp. 2257-2266
    • Linder, M.1    Szilvay, G.R.2    Nakari-Setälä, T.3    Soderlund, H.4    Penttilä, M.5
  • 100
    • 84899059237 scopus 로고    scopus 로고
    • A scale-up of hydrophobin-assisted recombinant protein production in tobacco BY-2 suspension cells
    • COI: 1:CAS:528:DC%2BC2cXmslOqtbs%3D
    • Reuter LJ, Bailey MJ, Joensuu JJ, Ritala A (2014) A scale-up of hydrophobin-assisted recombinant protein production in tobacco BY-2 suspension cells. Plant Biotech J 12:402–410
    • (2014) Plant Biotech J , vol.12 , pp. 402-410
    • Reuter, L.J.1    Bailey, M.J.2    Joensuu, J.J.3    Ritala, A.4
  • 101
    • 84920118132 scopus 로고    scopus 로고
    • Hydrophobins as aqueous lubricant additive for a soft sliding contact
    • COI: 1:CAS:528:DC%2BC2cXhvVOntrvK
    • Lee S, Røn T, Pakkanen KI, Linder M (2015) Hydrophobins as aqueous lubricant additive for a soft sliding contact. Colloids Surf B 125:264–269
    • (2015) Colloids Surf B , vol.125 , pp. 264-269
    • Lee, S.1    Røn, T.2    Pakkanen, K.I.3    Linder, M.4
  • 102
    • 0030053545 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the Trichoderma reesei hydrophobin HFBI
    • Nakari-Setälä T, Aro N, Kalkkinen N, Alatalo E, Penttilä M (1996) Genetic and biochemical characterization of the Trichoderma reesei hydrophobin HFBI. Eur J Biochem 235:248–255
    • (1996) Eur J Biochem , vol.235 , pp. 248-255
    • Nakari-Setälä, T.1    Aro, N.2    Kalkkinen, N.3    Alatalo, E.4    Penttilä, M.5
  • 103
    • 68649100000 scopus 로고    scopus 로고
    • The amphiphilic protein HFBII as a genetically taggable molecular carrier for the formation of a self-organized functional protein layer on a solid surface
    • COI: 1:CAS:528:DC%2BD1MXoslWls7c%3D
    • Asakawa H, Tahara S, Nakamichi M, Takehara K, Ikeno S, Linder MB, Haruyama T (2009) The amphiphilic protein HFBII as a genetically taggable molecular carrier for the formation of a self-organized functional protein layer on a solid surface. Langmuir 25:8841–8844
    • (2009) Langmuir , vol.25 , pp. 8841-8844
    • Asakawa, H.1    Tahara, S.2    Nakamichi, M.3    Takehara, K.4    Ikeno, S.5    Linder, M.B.6    Haruyama, T.7
  • 104
    • 33746064591 scopus 로고    scopus 로고
    • Two crystal structures of Trichoderma reesei hydrophobin HFBI—the structure of a protein amphiphile with and without detergent interaction
    • Hakanpää J, Szilvay GR, Kaljunen H, Maksimainen M, Linder MB, Rouvinen J (2006) Two crystal structures of Trichoderma reesei hydrophobin HFBI—the structure of a protein amphiphile with and without detergent interaction. Protein Sci 15(9):2129–2140
    • (2006) Protein Sci , vol.15 , Issue.9 , pp. 2129-2140
    • Hakanpää, J.1    Szilvay, G.R.2    Kaljunen, H.3    Maksimainen, M.4    Linder, M.B.5    Rouvinen, J.6
  • 105
    • 33646270402 scopus 로고    scopus 로고
    • Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A°
    • Hakanpaa J, Linder M, Popov A, Schmidt A, Rouvinen J (2006) Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A°. Acta Cryst 62:356–367
    • (2006) Acta Cryst , vol.62 , pp. 356-367
    • Hakanpaa, J.1    Linder, M.2    Popov, A.3    Schmidt, A.4    Rouvinen, J.5
  • 108
  • 113
    • 0034525882 scopus 로고    scopus 로고
    • Hydrophobins, unique fungal proteins
    • Wessels JGH (2000) Hydrophobins, unique fungal proteins. Mycologist 4:153–159
    • (2000) Mycologist , vol.4 , pp. 153-159
    • Wessels, J.G.H.1
  • 114
    • 84858760187 scopus 로고    scopus 로고
    • Creating surface properties using a palette of hydrophobins
    • COI: 1:CAS:528:DC%2BC3cXhtFGit7rJ
    • Zampieri F, Wösten HAB, Scholtmeijer K (2010) Creating surface properties using a palette of hydrophobins. Materials 3:4607–4625
    • (2010) Materials , vol.3 , pp. 4607-4625
    • Zampieri, F.1    Wösten, H.A.B.2    Scholtmeijer, K.3
  • 115
    • 84922473865 scopus 로고    scopus 로고
    • Applications of hydrophobins: current state and perspectives
    • Wösten HAB, Scholtmeijer K (2015) Applications of hydrophobins: current state and perspectives. Appl Microbiol Biot 99(4):1587–1597
    • (2015) Appl Microbiol Biot , vol.99 , Issue.4 , pp. 1587-1597
    • Wösten, H.A.B.1    Scholtmeijer, K.2
  • 120
    • 84861375022 scopus 로고    scopus 로고
    • Surface shear rheology of hydrophobin adsorption layers: laws of viscoelastic behaviour with applications to long-term foam stability
    • COI: 1:CAS:528:DC%2BC38XhsVehs73L
    • Danov KD, Radulova GM, Kralchevsky PA, Golemanov K, Stoyanov SD (2012) Surface shear rheology of hydrophobin adsorption layers: laws of viscoelastic behaviour with applications to long-term foam stability. Faraday Discuss 158:195–221
    • (2012) Faraday Discuss , vol.158 , pp. 195-221
    • Danov, K.D.1    Radulova, G.M.2    Kralchevsky, P.A.3    Golemanov, K.4    Stoyanov, S.D.5
  • 121
    • 84904696507 scopus 로고    scopus 로고
    • Competitive adsorption of the protein hydrophobin and an ionic surfactant: parallel vs sequential adsorption and dilatational rheology
    • COI: 1:CAS:528:DC%2BC2cXhtFyjsL7P
    • Stanimirova RD, Marinova KG, Danov KD, Kralchevsky PA, Basheva ES, Stoyanov SD, Pelan EG (2014) Competitive adsorption of the protein hydrophobin and an ionic surfactant: parallel vs sequential adsorption and dilatational rheology. Colloid Surf A 457:307–317
    • (2014) Colloid Surf A , vol.457 , pp. 307-317
    • Stanimirova, R.D.1    Marinova, K.G.2    Danov, K.D.3    Kralchevsky, P.A.4    Basheva, E.S.5    Stoyanov, S.D.6    Pelan, E.G.7
  • 123
    • 84874050353 scopus 로고    scopus 로고
    • Interfacial study of class II hydrophobin and its mixtures with milk proteins: relationship to bubble stability
    • COI: 1:CAS:528:DC%2BC3sXhtlWrsbo%3D
    • Wang Y, Bouillon C, Cox A, Dickinson E, Durga K, Murray BS, Xu R (2013) Interfacial study of class II hydrophobin and its mixtures with milk proteins: relationship to bubble stability. J Agric Food Chem 61:1554–1562
    • (2013) J Agric Food Chem , vol.61 , pp. 1554-1562
    • Wang, Y.1    Bouillon, C.2    Cox, A.3    Dickinson, E.4    Durga, K.5    Murray, B.S.6    Xu, R.7
  • 124
    • 84884418339 scopus 로고    scopus 로고
    • Interfacial rheology and stability of air bubbles stabilized by mixtures of hydrophobin and β-casein
    • COI: 1:CAS:528:DC%2BC3sXotVyj
    • Burke J, Cox A, Petkov J, Murray BS (2014) Interfacial rheology and stability of air bubbles stabilized by mixtures of hydrophobin and β-casein. Food Hydrocolloid 34:119–127
    • (2014) Food Hydrocolloid , vol.34 , pp. 119-127
    • Burke, J.1    Cox, A.2    Petkov, J.3    Murray, B.S.4
  • 125
    • 84900304602 scopus 로고    scopus 로고
    • Spontaneous surface self-assembly in protein-surfactant mixtures: interactions between hydrophobin and ethoxylated polysorbate surfactants
    • COI: 1:CAS:528:DC%2BC2cXmtlSmtLs%3D
    • Tucker IM, Petkov JT, Penfold J, Thomas RK, Li P, Cox AR, Hedges N, Webster JRP (2014) Spontaneous surface self-assembly in protein-surfactant mixtures: interactions between hydrophobin and ethoxylated polysorbate surfactants. J Phys Chem B 118:4867–4875
    • (2014) J Phys Chem B , vol.118 , pp. 4867-4875
    • Tucker, I.M.1    Petkov, J.T.2    Penfold, J.3    Thomas, R.K.4    Li, P.5    Cox, A.R.6    Hedges, N.7    Webster, J.R.P.8
  • 126
    • 80052246973 scopus 로고    scopus 로고
    • Adsorption behavior of hydrophobin and hydrophobin/surfactant mixtures at the solid-solution interface
    • COI: 1:CAS:528:DC%2BC3MXpvVersLk%3D
    • Zhang XL, Penfold J, Thomas RK, Tucker IM, Petkov JT, Bent J, Cox A (2011) Adsorption behavior of hydrophobin and hydrophobin/surfactant mixtures at the solid-solution interface. Langmuir 27:10464–10474
    • (2011) Langmuir , vol.27 , pp. 10464-10474
    • Zhang, X.L.1    Penfold, J.2    Thomas, R.K.3    Tucker, I.M.4    Petkov, J.T.5    Bent, J.6    Cox, A.7
  • 127
    • 80052199843 scopus 로고    scopus 로고
    • Self-assembly of hydrophobin and hydrophobin/surfactant mixtures in aqueous solution
    • COI: 1:CAS:528:DC%2BC3MXpsVOhu70%3D
    • Zhang XL, Penfold J, Thomas RK, Tucker IM, Petkov JT, Bent J, Cox A, Grillo I (2011) Self-assembly of hydrophobin and hydrophobin/surfactant mixtures in aqueous solution. Langmuir 27:10514–10522
    • (2011) Langmuir , vol.27 , pp. 10514-10522
    • Zhang, X.L.1    Penfold, J.2    Thomas, R.K.3    Tucker, I.M.4    Petkov, J.T.5    Bent, J.6    Cox, A.7    Grillo, I.8
  • 128
    • 80052720342 scopus 로고    scopus 로고
    • Adsorption behavior of hydrophobin and hydrophobin/surfactant mixtures at the air–water interface
    • COI: 1:CAS:528:DC%2BC3MXhtVGnu7bJ
    • Zhang XL, Penfold J, Thomas RK, Tucker IM, Petkov JT, Bent J, Cox A, Campbell RA (2011) Adsorption behavior of hydrophobin and hydrophobin/surfactant mixtures at the air–water interface. Langmuir 27:11316–11323
    • (2011) Langmuir , vol.27 , pp. 11316-11323
    • Zhang, X.L.1    Penfold, J.2    Thomas, R.K.3    Tucker, I.M.4    Petkov, J.T.5    Bent, J.6    Cox, A.7    Campbell, R.A.8
  • 130
    • 84973354664 scopus 로고    scopus 로고
    • Foaming agents comprising hydrophobin
    • Cox AR (2013) Foaming agents comprising hydrophobin. Patent US 20130216655 A1
    • (2013) Patent US , pp. A1
    • Cox, A.R.1
  • 136
    • 84891847668 scopus 로고    scopus 로고
    • Hydrophobin-coated plates as matrix-assisted laser desorption/ionization sample support for peptide/protein analysis
    • COI: 1:CAS:528:DC%2BC2cXisFChsb0%3D
    • Longobardi S, Gravagnuolo AM, Rea I, De Stefano L, Marino G, Giardina P (2014) Hydrophobin-coated plates as matrix-assisted laser desorption/ionization sample support for peptide/protein analysis. Anal Biochem 449:9–16
    • (2014) Anal Biochem , vol.449 , pp. 9-16
    • Longobardi, S.1    Gravagnuolo, A.M.2    Rea, I.3    De Stefano, L.4    Marino, G.5    Giardina, P.6
  • 139
    • 52949117137 scopus 로고    scopus 로고
    • Isolation of the orthologue of the cerato-ulmin gene in Ophiostoma quercus and characterization of the purified protein
    • COI: 1:CAS:528:DC%2BD1cXhsV2ktr7M
    • Carresi L, Comparini C, Bettini PP, Pazzagli L, Cappugi G, Scala F, Scala A (2008) Isolation of the orthologue of the cerato-ulmin gene in Ophiostoma quercus and characterization of the purified protein. Mycol Res 112:1245–1255
    • (2008) Mycol Res , vol.112 , pp. 1245-1255
    • Carresi, L.1    Comparini, C.2    Bettini, P.P.3    Pazzagli, L.4    Cappugi, G.5    Scala, F.6    Scala, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.