메뉴 건너뛰기




Volumn 10, Issue 80, 2013, Pages

Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Author keywords

Adsorption; Interface; Neutron reflectometry; Peptide; Protein; Rheology

Indexed keywords

ADSORPTION; ELASTICITY; INTERFACES (MATERIALS); MONOLAYERS; NEUTRON REFLECTION; PEPTIDES; PROTEINS; RHEOLOGY;

EID: 84920506286     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2012.0987     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 77955770512 scopus 로고    scopus 로고
    • New views on foams from protein solutions
    • doi:10.1016/j.cocis.2010.05.017
    • Wierenga PA, Gruppen H. 2010 New views on foams from protein solutions. Curr. Opin. Colloid Interface Sci. 15, 365-373. (doi:10.1016/j.cocis.2010.05. 017).
    • (2010) Curr. Opin. Colloid Interface Sci. , vol.15 , pp. 365-373
    • Wierenga, P.A.1    Gruppen, H.2
  • 3
    • 37049084567 scopus 로고
    • Coalescence stability of emulsion-sized droplets at a planar oil-water interface and the relationship to protein film surface rheology
    • doi:10.1039/f19888400871
    • Dickinson E, Murray BS, Stainsby G. 1988 Coalescence stability of emulsion-sized droplets at a planar oil-water interface and the relationship to protein film surface rheology. J. Chem. Soc. Faraday Trans. I 84, 871-883. (doi:10.1039/f19888400871).
    • (1988) J. Chem. Soc. Faraday Trans. I , vol.84 , pp. 871-883
    • Dickinson, E.1    Murray, B.S.2    Stainsby, G.3
  • 4
    • 75449087522 scopus 로고    scopus 로고
    • PH Influence on the stability of foams with protein- polysaccharide complexes at their interfaces
    • doi:10.1016/j.foodhyd. 2009.11.006
    • Miquelim JN, Lannes SCS, Mezzenga R. 2010 pH Influence on the stability of foams with protein- polysaccharide complexes at their interfaces. Food Hydrocolloids 24, 398-405. (doi:10.1016/j.foodhyd. 2009.11.006).
    • (2010) Food Hydrocolloids , vol.24 , pp. 398-405
    • Miquelim, J.N.1    Lannes, S.C.S.2    Mezzenga, R.3
  • 5
    • 33747589008 scopus 로고    scopus 로고
    • Interfacial and foaming properties of sulfydrylmodified bovine beta-lactoglobulin
    • doi:10.1016/j.jcis. 2006.06.061
    • Croguennec T, Renault A, Bouhallab S, Pezennec S. 2006 Interfacial and foaming properties of sulfydrylmodified bovine beta-lactoglobulin. J. Colloid Interface Sci. 302, 32-39. (doi:10.1016/j.jcis. 2006.06.061).
    • (2006) J. Colloid Interface Sci. , vol.302 , pp. 32-39
    • Croguennec, T.1    Renault, A.2    Bouhallab, S.3    Pezennec, S.4
  • 6
    • 67149102424 scopus 로고    scopus 로고
    • Effect of transglutaminase-induced cross-linking of sodium caseinate on the properties of equilibrated interfaces and foams
    • doi:10.1016/j.colsurfa. 2009.02.004
    • Partanen R, Paananen A, Forssell P, Linder MB, Lille M, Buchert J, Lantto R. 2009 Effect of transglutaminase-induced cross-linking of sodium caseinate on the properties of equilibrated interfaces and foams. Colloid Surf. A Physicochem. Eng. Asp. 344, 79-85. (doi:10.1016/j.colsurfa. 2009.02.004).
    • (2009) Colloid Surf. A Physicochem. Eng. Asp. , vol.344 , pp. 79-85
    • Partanen, R.1    Paananen, A.2    Forssell, P.3    Linder, M.B.4    Lille, M.5    Buchert, J.6    Lantto, R.7
  • 7
    • 0036403301 scopus 로고    scopus 로고
    • Network forming properties of various proteins adsorbed at the air/water interface in relation to foam stability
    • doi:10.1006/jcis.2002.8592
    • Martin AH, Grolle K, Bos MA, Stuart MA, van Vliet T. 2002 Network forming properties of various proteins adsorbed at the air/water interface in relation to foam stability. J. Colloid Interface Sci. 254, 175-183. (doi:10.1006/jcis. 2002.8592).
    • (2002) J. Colloid Interface Sci. , vol.254 , pp. 175-183
    • Martin, A.H.1    Grolle, K.2    Bos, M.A.3    Stuart, M.A.4    Van Vliet, T.5
  • 8
    • 33846357146 scopus 로고    scopus 로고
    • Comparisons of the foaming and interfacial properties of whey protein isolate and egg white proteins
    • doi:10.1016/j.colsurfb. 2006.10.017
    • Davis JP, Foegeding EA. 2007 Comparisons of the foaming and interfacial properties of whey protein isolate and egg white proteins. Colloid Surf. B Biointerfaces 54, 200-210. (doi:10.1016/j.colsurfb. 2006.10.017).
    • (2007) Colloid Surf. B Biointerfaces , vol.54 , pp. 200-210
    • Davis, J.P.1    Foegeding, E.A.2
  • 9
    • 78751706080 scopus 로고    scopus 로고
    • Rheological properties of protein films
    • doi:10.1016/j.cocis.2010.06.005
    • Murray BS. 2011 Rheological properties of protein films. Curr. Opin. Colloid Interface Sci. 16, 27-35. (doi:10.1016/j.cocis.2010.06.005).
    • (2011) Curr. Opin. Colloid Interface Sci. , vol.16 , pp. 27-35
    • Murray, B.S.1
  • 10
    • 0028250433 scopus 로고
    • Deamidation of food proteins to improve functionality
    • doi:10.1080/10408399409527664
    • Hamada JS, Swanson B. 1994 Deamidation of food proteins to improve functionality. Crit. Rev. Food Sci. Nutr. 34, 283-292. (doi:10.1080/ 10408399409527664).
    • (1994) Crit. Rev. Food Sci. Nutr. , vol.34 , pp. 283-292
    • Hamada, J.S.1    Swanson, B.2
  • 11
    • 20344376903 scopus 로고    scopus 로고
    • Foaming and interfacial properties of hydrolyzed b-lactoglobulin
    • doi:10.1016/j.jcis.2005.03.002
    • Davis JP, Doucet D, Foegeding EA. 2005 Foaming and interfacial properties of hydrolyzed b-lactoglobulin. J. Colloid Interface Sci. 288, 412-422. (doi:10.1016/j.jcis.2005.03.002).
    • (2005) J. Colloid Interface Sci. , vol.288 , pp. 412-422
    • Davis, J.P.1    Doucet, D.2    Foegeding, E.A.3
  • 12
    • 0030127886 scopus 로고    scopus 로고
    • Enhancing the functionality of food proteins by enzymatic modification
    • doi:10.1016/0924-2244(96)10012-1
    • Panyam D, Kilara A. 1996 Enhancing the functionality of food proteins by enzymatic modification. Trends Food Sci. Technol. 7, 120-125. (doi:10.1016/0924-2244(96)10012-1).
    • (1996) Trends Food Sci. Technol. , vol.7 , pp. 120-125
    • Panyam, D.1    Kilara, A.2
  • 13
    • 0036589178 scopus 로고    scopus 로고
    • Advances in modifying and understanding whey protein functionality
    • doi:10.1016/s0924-2244 (02)00111-5
    • Foegeding EA, Davis JP, Doucet D, McGuffey MK. 2002 Advances in modifying and understanding whey protein functionality. Trends Food Sci. Technol. 13, 151-159. (doi:10.1016/s0924-2244 (02)00111-5).
    • (2002) Trends Food Sci. Technol. , vol.13 , pp. 151-159
    • Foegeding, E.A.1    Davis, J.P.2    Doucet, D.3    Mcguffey, M.K.4
  • 14
    • 79952112477 scopus 로고    scopus 로고
    • Interfacial activity and interfacial shear rheology of native beta-lactoglobulin monomers and their heatinduced fibers
    • doi:10.1021/la102721m
    • Jung JM, Gunes DZ, Mezzenga R. 2010 Interfacial activity and interfacial shear rheology of native beta-lactoglobulin monomers and their heatinduced fibers. Langmuir 26, 15 366-15 375. (doi:10.1021/la102721m).
    • (2010) Langmuir , vol.26 , pp. 15366-15375
    • Jung, J.M.1    Gunes, D.Z.2    Mezzenga, R.3
  • 15
    • 79957570728 scopus 로고    scopus 로고
    • A designed biosurfactant protein for switchable foam control
    • doi:10. 1002/cphc.201100082
    • Middelberg APJ, Dimitrijev-Dwyer M. 2011 A designed biosurfactant protein for switchable foam control. ChemPhysChem 12, 1426-1429. (doi:10. 1002/cphc.201100082).
    • (2011) ChemPhysChem , vol.12 , pp. 1426-1429
    • Middelberg, A.P.J.1    Dimitrijev-Dwyer, M.2
  • 16
    • 84860362296 scopus 로고    scopus 로고
    • The effects of acid hydrolysis on protein biosurfactant molecular, interfacial, and foam properties: PH responsive protein hydrolysates
    • doi:10.1039/c2sm25082a
    • Dimitrijev-Dwyer M, He LZ, James M, Nelson A, Wang LG, Middelberg APJ. 2012 The effects of acid hydrolysis on protein biosurfactant molecular, interfacial, and foam properties: pH responsive protein hydrolysates. Soft Matter 8, 5131-5139. (doi:10.1039/c2sm25082a).
    • (2012) Soft Matter , vol.8 , pp. 5131-5139
    • Dimitrijev-Dwyer, M.1    He, L.Z.2    James, M.3    Nelson, A.4    Wang, L.G.5    Middelberg, A.P.J.6
  • 17
    • 33744780455 scopus 로고    scopus 로고
    • Reversible active switching of the mechanical properties of a peptide film at a fluid-fluid interface
    • doi:10.1038/nmat1653
    • Dexter AF, Malcolm AS, Middelberg APJ. 2006 Reversible active switching of the mechanical properties of a peptide film at a fluid-fluid interface. Nat. Mater. 5, 502-506. (doi:10.1038/nmat1653).
    • (2006) Nat. Mater. , vol.5 , pp. 502-506
    • Dexter, A.F.1    Malcolm, A.S.2    Middelberg, A.P.J.3
  • 18
    • 36348987628 scopus 로고    scopus 로고
    • The interfacial structure and Young's modulus of peptide films having switchable mechanical properties
    • doi:10.1098/rsif.2007.1063
    • Middelberg A, He L, Dexter A, Shen H, Holt S, Thomas R. 2008 The interfacial structure and Young's modulus of peptide films having switchable mechanical properties. J. R. Soc. Interface 5, 47-54. (doi:10.1098/rsif.2007. 1063).
    • (2008) J. R. Soc. Interface , vol.5 , pp. 47-54
    • Middelberg, A.1    He, L.2    Dexter, A.3    Shen, H.4    Holt, S.5    Thomas, R.6
  • 19
    • 34547531123 scopus 로고    scopus 로고
    • Switchable peptide surfactants with designed metal binding capacity
    • doi:10.1021/jp071554s
    • Dexter AF, Middelberg APJ. 2007 Switchable peptide surfactants with designed metal binding capacity. J. Phys. Chem. C 111, 10 484-10 492. (doi:10.1021/jp071554s).
    • (2007) J. Phys. Chem. C , vol.111 , pp. 10484-10492
    • Dexter, A.F.1    Middelberg, A.P.J.2
  • 20
    • 0343036207 scopus 로고    scopus 로고
    • Determination of equilibrium surface tension values by extrapolation via long time approximations
    • doi:10. 1016/s0927-7757(96)03857-5
    • Makievski AV, Fainerman VB, Miller R, Bree M, Liggieri L, Ravera F. 1997 Determination of equilibrium surface tension values by extrapolation via long time approximations. Colloid Surf. A Physicochem. Eng. Asp. 122, 269-273. (doi:10. 1016/s0927-7757(96)03857-5).
    • (1997) Colloid Surf. A Physicochem. Eng. Asp. , vol.122 , pp. 269-273
    • Makievski, A.V.1    Fainerman, V.B.2    Miller, R.3    Bree, M.4    Liggieri, L.5    Ravera, F.6
  • 21
    • 0034625006 scopus 로고    scopus 로고
    • Peptide interfacial adsorption is kinetically limited by the thermodynamic stability of self association
    • doi:10.1073/pnas.080042597
    • Middelberg APJ, Radke CJ, Blanch HW. 2000 Peptide interfacial adsorption is kinetically limited by the thermodynamic stability of self association. Proc. Natl Acad. Sci. USA 97, 5054-5059. (doi:10.1073/pnas.080042597).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5054-5059
    • Middelberg, A.P.J.1    Radke, C.J.2    Blanch, H.W.3
  • 22
    • 0025388039 scopus 로고
    • Prediction of diffusion coefficients of proteins
    • doi:10.1002/bit.260350402
    • Tyn MT, Gusek TW. 1990 Prediction of diffusion coefficients of proteins. Biotechnol. Bioeng. 35, 327-338. (doi:10.1002/bit.260350402).
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 327-338
    • Tyn, M.T.1    Gusek, T.W.2
  • 23
    • 79953759979 scopus 로고    scopus 로고
    • Motofit-integrating neutron reflectometry acquisition, reduction and analysis into one, easy to use, package
    • doi:10.1088/1742-6596/251/1/012094
    • Nelson A. 2010 Motofit-integrating neutron reflectometry acquisition, reduction and analysis into one, easy to use, package. J. Phys.: Conf. Ser. 251, 012094. (doi:10.1088/1742-6596/251/1/012094).
    • (2010) J. Phys.: Conf. Ser. , vol.251 , pp. 012094
    • Nelson, A.1
  • 25
    • 33645140429 scopus 로고    scopus 로고
    • Co-refinement of multiple-contrast neutron/X-ray reflectivity data using MOTOFIT
    • doi:10.1107/S0021889806005073
    • Nelson A. 2006 Co-refinement of multiple-contrast neutron/X-ray reflectivity data using MOTOFIT. J. Appl. Crystallogr. 39, 273-276. (doi:10.1107/S0021889806005073).
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 273-276
    • Nelson, A.1
  • 26
    • 84915486634 scopus 로고
    • Neutron scattering lengths and cross sections
    • doi:10.1080/10448639208218770
    • Sears VF. 1992 Neutron scattering lengths and cross sections. Neutron News 3, 26-37. (doi:10.1080/10448639208218770).
    • (1992) Neutron News , vol.3 , pp. 26-37
    • Sears, V.F.1
  • 27
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • doi:10.1002/bip.1981.360201110
    • Jacrot B, Zaccai G. 1981 Determination of molecular weight by neutron scattering. Biopolymers 20, 2413-2426. (doi:10.1002/bip.1981.360201110).
    • (1981) Biopolymers , vol.20 , pp. 2413-2426
    • Jacrot, B.1    Zaccai, G.2
  • 28
    • 65249129772 scopus 로고    scopus 로고
    • Cooperative tuneable interactions between a designed peptide biosurfactant and positional isomers of SDOBS at the air-water interface
    • doi:10.1021/la802825c
    • He LZ, Malcolm AS, Dimitrijev M, Onaizi SA, Shen HH, Holt SA, Dexter AF, Thomas RK, Middelberg APJ. 2009 Cooperative tuneable interactions between a designed peptide biosurfactant and positional isomers of SDOBS at the air-water interface. Langmuir 25, 4021-4026. (doi:10.1021/la802825c).
    • (2009) Langmuir , vol.25 , pp. 4021-4026
    • He, L.Z.1    Malcolm, A.S.2    Dimitrijev, M.3    Onaizi, S.A.4    Shen, H.H.5    Holt, S.A.6    Dexter, A.F.7    Thomas, R.K.8    Middelberg, A.P.J.9
  • 29
    • 0037118274 scopus 로고    scopus 로고
    • Direct determination of the mechanical properties of an interfacially adsorbed protein film
    • doi:10.1016/S0009- 2509(02)00057-X
    • Jones DB, Middelberg APJ. 2002 Direct determination of the mechanical properties of an interfacially adsorbed protein film. Chem. Eng. Sci. 57, 1711-1722. (doi:10.1016/S0009- 2509(02)00057-X).
    • (2002) Chem. Eng. Sci. , vol.57 , pp. 1711-1722
    • Jones, D.B.1    Middelberg, A.P.J.2
  • 30
    • 0035880019 scopus 로고    scopus 로고
    • Kinetics of adsorption of globular proteins at liquid/fluid interfaces
    • doi:10.1016/s0927- 7757(01)00523-4
    • Miller R, Aksenenko EV, Fainerman VB, Pison U. 2001 Kinetics of adsorption of globular proteins at liquid/fluid interfaces. Colloid Surf. A Physicochem. Eng. Asp. 183, 381-390. (doi:10.1016/s0927- 7757(01)00523-4).
    • (2001) Colloid Surf. A Physicochem. Eng. Asp. , vol.183 , pp. 381-390
    • Miller, R.1    Aksenenko, E.V.2    Fainerman, V.B.3    Pison, U.4
  • 31
    • 3342914945 scopus 로고    scopus 로고
    • Neutron reflection from liquid interfaces
    • doi:10.1146/annurev.physchem.54.011002.103830
    • Thomas RK. 2004 Neutron reflection from liquid interfaces. Annu. Rev. Phys. Chem. 55, 391-426. (doi:10.1146/annurev.physchem.54.011002.103830).
    • (2004) Annu. Rev. Phys. Chem. , vol.55 , pp. 391-426
    • Thomas, R.K.1
  • 32
    • 82455164803 scopus 로고    scopus 로고
    • Relationship between surface tension and surface coverage
    • doi:10.1021/la203009m
    • Menger FM, Rizvi SAA. 2011 Relationship between surface tension and surface coverage. Langmuir 27, 13 975-13 977. (doi:10.1021/la203009m).
    • (2011) Langmuir , vol.27 , pp. 13975-13977
    • Menger, F.M.1    Rizvi, S.A.A.2
  • 33
    • 49249153429 scopus 로고
    • Proteins at liquid interfaces. 1. Kinetics of adsorption and surface denaturation
    • doi:10.1016/0021-9797(79)90048-1
    • Graham DE, Phillips MC. 1979 Proteins at liquid interfaces. 1. Kinetics of adsorption and surface denaturation. J. Colloid Interface Sci. 70, 403-414. (doi:10.1016/0021-9797(79)90048-1).
    • (1979) J. Colloid Interface Sci. , vol.70 , pp. 403-414
    • Graham, D.E.1    Phillips, M.C.2
  • 34
    • 51049118989 scopus 로고    scopus 로고
    • Synergy between ovalbumin and lysozyme leads to non-additive interfacial and foaming properties of mixtures
    • doi:10.1016/j.foodhyd.2008.01.007
    • Le Floch-Fouere C, Pezennec S, Lechevalier V, Beaufils S, Desbat B, Pezolet M, Renault A. 2009 Synergy between ovalbumin and lysozyme leads to non-additive interfacial and foaming properties of mixtures. Food Hydrocolloids 23, 352-365. (doi:10.1016/j.foodhyd.2008.01.007).
    • (2009) Food Hydrocolloids , vol.23 , pp. 352-365
    • Le, F.-F.C.1    Pezennec, S.2    Lechevalier, V.3    Beaufils, S.4    Desbat, B.5    Pezolet, M.6    Renault, A.7
  • 35
    • 0033828828 scopus 로고    scopus 로고
    • The protein net electric charge determines the surface rheological properties of ovalbumin adsorbed at the air-water interface
    • doi:10.1016/S0268-005X(00)00026-6
    • Pezennec S, Gauthier F, Alonso C, Graner F, Croguennec T, Brule G, Renault A. 2000 The protein net electric charge determines the surface rheological properties of ovalbumin adsorbed at the air-water interface. Food Hydrocolloids 14, 463-472. (doi:10.1016/S0268-005X(00)00026-6).
    • (2000) Food Hydrocolloids , vol.14 , pp. 463-472
    • Pezennec, S.1    Gauthier, F.2    Alonso, C.3    Graner, F.4    Croguennec, T.5    Brule, G.6    Renault, A.7
  • 36
    • 23444448540 scopus 로고    scopus 로고
    • Combined surface pressure-interfacial shear rheology study of the effect of pH on the adsorption of proteins at the air-water interface
    • doi:10.1021/la050272l
    • Roberts SA, Kellaway IW, Taylor KMG, Warburton B, Peters K. 2005 Combined surface pressure-interfacial shear rheology study of the effect of pH on the adsorption of proteins at the air-water interface. Langmuir 21, 7342-7348. (doi:10.1021/la050272l).
    • (2005) Langmuir , vol.21 , pp. 7342-7348
    • Roberts, S.A.1    Kellaway, I.W.2    Taylor, K.M.G.3    Warburton, B.4    Peters, K.5
  • 37
    • 33750356658 scopus 로고    scopus 로고
    • Mechanical properties of interfacial films formed by lysozyme self-assembly at the air-water interface
    • doi:10.1021/la060565u
    • Malcolm AS, Dexter AF, Middelberg APJ. 2006 Mechanical properties of interfacial films formed by lysozyme self-assembly at the air-water interface. Langmuir 22, 8897-8905. (doi:10.1021/la060565u).
    • (2006) Langmuir , vol.22 , pp. 8897-8905
    • Malcolm, A.S.1    Dexter, A.F.2    Middelberg, A.P.J.3
  • 38
    • 84856034675 scopus 로고    scopus 로고
    • The extensional viscoelasticity of protein-coated interfaces
    • doi:10.1039/c1sm05253e
    • Dimitrijev-Dwyer M, Middelberg APJ. 2011 The extensional viscoelasticity of protein-coated interfaces. Soft Matter 7, 7772-7781. (doi:10.1039/c1sm05253e) .
    • (2011) Soft Matter , vol.7 , pp. 7772-7781
    • Dimitrijev-Dwyer, M.1    Middelberg, A.P.J.2
  • 39
    • 6744235691 scopus 로고
    • The role of short chain molecules for the rheology of polystyrene melts. I. Molar mass dependent shift factors
    • doi:10.1007/bf01333847
    • Knoglinger H, Schausberger A, Janeschitzkriegl H. 1987 The role of short chain molecules for the rheology of polystyrene melts. I. Molar mass dependent shift factors. Rheol. Acta 26, 460-467. (doi:10.1007/bf01333847).
    • (1987) Rheol. Acta , vol.26 , pp. 460-467
    • Knoglinger, H.1    Schausberger, A.2    Janeschitzkriegl, H.3
  • 40
    • 0024622714 scopus 로고
    • Infrared dichroism measurement of molecular relaxation in binary blend melt rheology
    • doi:10.1021/ma00193a055
    • Kornfield JA, Fuller GG, Pearson DS. 1989 Infrared dichroism measurement of molecular relaxation in binary blend melt rheology. Macromolecules 22, 1334-1345. (doi:10.1021/ma00193a055).
    • (1989) Macromolecules , vol.22 , pp. 1334-1345
    • Kornfield, J.A.1    Fuller, G.G.2    Pearson, D.S.3
  • 41
    • 4243049126 scopus 로고
    • The role of short chain molecules for the rheology of polystyrene melts. II. Linear viscoelastic properties
    • doi:10.1007/bf01333848
    • Schausberger A, Knoglinger H, Janeschitzkriegl H. 1987 The role of short chain molecules for the rheology of polystyrene melts. II. Linear viscoelastic properties. Rheol. Acta 26, 468-473. (doi:10.1007/bf01333848).
    • (1987) Rheol. Acta , vol.26 , pp. 468-473
    • Schausberger, A.1    Knoglinger, H.2    Janeschitzkriegl, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.