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Volumn 17, Issue 7, 2007, Pages 846-853

Heat-induced whey protein isolate fibrils: Conversion, hydrolysis, and disulphide bond formation

Author keywords

Conversion; Fibrils; Heat induced aggregation; HPLC; SDS PAGE; Whey proteins

Indexed keywords

HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; IONIC STRENGTH; MONOMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRECIPITATION (CHEMICAL);

EID: 33947694371     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2006.10.002     Document Type: Article
Times cited : (126)

References (14)
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    • Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2
    • Aymard P., Nicolai T., Durand D., and Clark A. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules 32 (1999) 2542-2552
    • (1999) Macromolecules , vol.32 , pp. 2542-2552
    • Aymard, P.1    Nicolai, T.2    Durand, D.3    Clark, A.4
  • 6
    • 0036196674 scopus 로고    scopus 로고
    • Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy
    • Ikeda S., and Morris V.J. Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules 3 (2002) 382-389
    • (2002) Biomacromolecules , vol.3 , pp. 382-389
    • Ikeda, S.1    Morris, V.J.2
  • 8
    • 33947644406 scopus 로고    scopus 로고
    • Rogers, S. S. (2006). Some Physical Properties of Amyloid Fibrils. Ph.D. thesis, Biological and Soft Systems, Cavendish Laboratory, Cambridge University, UK.
  • 9
    • 17044440175 scopus 로고    scopus 로고
    • Measuring length distribution of a fibril system: A flow birefringence technique applied to amyloid fibrils
    • Rogers S.S., Venema P., Sagis L.M.C., van der Linden E., and Donald A.M. Measuring length distribution of a fibril system: A flow birefringence technique applied to amyloid fibrils. Macromolecules 38 (2005) 2948-2958
    • (2005) Macromolecules , vol.38 , pp. 2948-2958
    • Rogers, S.S.1    Venema, P.2    Sagis, L.M.C.3    van der Linden, E.4    Donald, A.M.5
  • 10
    • 0033846408 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 influenced by ionic strength and protein concentration
    • Schokker E.P., Singh H., Pinder D.N., and Creamer L.K. Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 influenced by ionic strength and protein concentration. International Dairy Journal 10 (2000) 233-240
    • (2000) International Dairy Journal , vol.10 , pp. 233-240
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Creamer, L.K.4
  • 12
    • 0036054901 scopus 로고    scopus 로고
    • Effect of electrostatic interactions on the percolation concentration of fibrillar β-lactoglobulin gels
    • Veerman C., Ruis H., Sagis L.M.C., and van der Linden E. Effect of electrostatic interactions on the percolation concentration of fibrillar β-lactoglobulin gels. Biomacromolecules 3 (2002) 869-873
    • (2002) Biomacromolecules , vol.3 , pp. 869-873
    • Veerman, C.1    Ruis, H.2    Sagis, L.M.C.3    van der Linden, E.4
  • 13
    • 33947692309 scopus 로고    scopus 로고
    • Verheul, M. (1997). Aggregation and gelation of whey proteins. Ph.D. thesis, Rheology Group, Universiteit Twente, The Netherlands.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.