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Volumn 38, Issue 4, 2014, Pages 129-134

Biophysical characterisation of hydrophobin enriched foamate

Author keywords

Foam; Hydrophobin; Surface tension

Indexed keywords

FOAMS; SURFACE TENSION;

EID: 84902547816     PISSN: 13737163     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cervis.2014.04.003     Document Type: Article
Times cited : (8)

References (27)
  • 2
    • 37849008156 scopus 로고    scopus 로고
    • Ochratoxin A production in relation to ecophysiological factors by Aspergillus section Nigri strains isolated from different substrates in Argentina
    • A. Astoreca, C. Magnoli, C. Barberis, S.M. Chiacchiera, M. Combina, and A. Dalcero Ochratoxin A production in relation to ecophysiological factors by Aspergillus section Nigri strains isolated from different substrates in Argentina Sci. Total Environ. 388 2007 16 23
    • (2007) Sci. Total Environ. , vol.388 , pp. 16-23
    • Astoreca, A.1    Magnoli, C.2    Barberis, C.3    Chiacchiera, S.M.4    Combina, M.5    Dalcero, A.6
  • 5
    • 33749051927 scopus 로고    scopus 로고
    • Thermal Stability of Proteins
    • J.C. Bischof, and X. He Thermal Stability of Proteins Ann. NY. Acad. Sci. 1066 2005 12 33
    • (2005) Ann. NY. Acad. Sci. , vol.1066 , pp. 12-33
    • Bischof, J.C.1    He, X.2
  • 6
    • 77950822737 scopus 로고    scopus 로고
    • On the link between foam coarsening and surface rheology: Why hydrophobins are so different
    • T.B.J. Blijdenstein, P.W.N. de Groot, and S.D. Stoyanov On the link between foam coarsening and surface rheology: why hydrophobins are so different Soft Matter. 6 2010 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
  • 7
    • 51049104790 scopus 로고    scopus 로고
    • Exceptional stability of food foams using class II hydrophobin HFBII
    • A.R. Cox, D.L. Aldred, and A.B. Russell Exceptional stability of food foams using class II hydrophobin HFBII Food Hydrocolloid. 23 2009 366 376
    • (2009) Food Hydrocolloid. , vol.23 , pp. 366-376
    • Cox, A.R.1    Aldred, D.L.2    Russell, A.B.3
  • 11
    • 33746064591 scopus 로고    scopus 로고
    • Two crystal structures of Trichoderma reesei hydrophobin HFBI - The structure of a protein amphiphile with and without detergent interaction
    • DOI 10.1110/ps.062326706
    • J. Hakanpaa, G.R. Szilvay, H. Kaljunen, M. Maksimainen, M. Linder, and J. Rouvinen Two crystal structures of Trichoderma reesei hydrophobin HFBI - The structure of a protein amphiphile with and without detergent interaction Protein Sci. 15 2006 2129 2140 (Pubitemid 44316015)
    • (2006) Protein Science , vol.15 , Issue.9 , pp. 2129-2140
    • Hakanpaa, J.1    Szilvay, G.R.2    Kaljunen, H.3    Maksimainen, M.4    Linder, M.5    Rouvinen, J.6
  • 13
    • 84862296168 scopus 로고    scopus 로고
    • Hydrophobins: Exceptional proteins for many applications in brewery environment and other bio-industries
    • M. Khalesi, S.M. Deckers, K. Gebreurs, L. Vissers, H. Verachtert, and G. Derdenlickx Hydrophobins: exceptional proteins for many applications in brewery environment and other bio-industries Cerevisia 37 2012 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
  • 15
    • 84872529533 scopus 로고    scopus 로고
    • The effects of temperature and relative humidity on ochratoxin A formation in fresh liquorice root
    • M. Khalesi, M. Tabrizchi, and M. Sheikh-Zeinoddin The effects of temperature and relative humidity on ochratoxin A formation in fresh liquorice root Food Addit. Contam. A. 30 2013 339 344
    • (2013) Food Addit. Contam. A. , vol.30 , pp. 339-344
    • Khalesi, M.1    Tabrizchi, M.2    Sheikh-Zeinoddin, M.3
  • 16
    • 53249093907 scopus 로고    scopus 로고
    • Mechanisms of aqueous foam stability and antifoaming action
    • Y.H. Kim, and C.U. Kim Mechanisms of aqueous foam stability and antifoaming action J. Ind. Eng. Chem. 3 1997 138 146
    • (1997) J. Ind. Eng. Chem. , vol.3 , pp. 138-146
    • Kim, Y.H.1    Kim, C.U.2
  • 17
    • 37749006898 scopus 로고    scopus 로고
    • Interactions of Hydrophobin Proteins in Solution Studied by Small-Angle X-Ray Scattering
    • K. Kisko, G.R. Szilvay, U. Vainio, M.B. Linder, and R. Serimaa Interactions of Hydrophobin Proteins in Solution Studied by Small-Angle X-Ray Scattering Biophysical J. 94 2008 198 206
    • (2008) Biophysical J. , vol.94 , pp. 198-206
    • Kisko, K.1    Szilvay, G.R.2    Vainio, U.3    Linder, M.B.4    Serimaa, R.5
  • 18
    • 34047167038 scopus 로고    scopus 로고
    • Isolation and bioactivity of an angiogenesis inhibitor extracted from the cartilage of Dasyatis akajei
    • H. Luo, J. Xu, and X. Yu Isolation and bioactivity of an angiogenesis inhibitor extracted from the cartilage of Dasyatis akajei Asia Pac. J. Clin. Nutr. 16 2007 286 289 (Pubitemid 46524616)
    • (2007) Asia Pacific Journal of Clinical Nutrition , vol.16 , Issue.SUPPL.1 , pp. 286-289
    • Luo, H.1    Xu, J.2    Yu, X.3
  • 19
    • 41149142438 scopus 로고    scopus 로고
    • Study on sodium caseinate foam stability by multiple light scattering
    • DOI 10.1177/1082013207087815
    • P. Sceni, and J.R. Wagner Study on Sodium Caseinate Foam Stability by Multiple Light Scattering Food Sci. Technol. Int. 13 2007 461 468 (Pubitemid 351433410)
    • (2007) Food Science and Technology International , vol.13 , Issue.6 , pp. 461-468
    • Wagner, J.R.1    Sceni, P.2
  • 26
    • 17844399807 scopus 로고    scopus 로고
    • The SC3 hydrophobin self-assembles into a membrane with distinct mass transfer properties
    • DOI 10.1529/biophysj.104.057794
    • X. Wang, F. Shi, H.A.B. Wösten, H. Hektor, B. Poolman, and G.T. Robillard The SC3 Hydrophobin Self-Assembles into a Membrane with Distinct Mass Transfer Properties Biophysical J. 88 2005 3434 3443 (Pubitemid 40586593)
    • (2005) Biophysical Journal , vol.88 , Issue.5 , pp. 3434-3443
    • Wang, X.1    Shi, F.2    Wosten, H.A.B.3    Hektor, H.4    Poolman, B.5    Robillard, G.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.