Fibrillar structures in food

作者: Ardy Kroes-Nijboer , Paul Venema , Erik van der Linden

DOI: 10.1039/C1FO10163C

关键词:

摘要: Assembly of proteins or peptides into fibrils is an important subject study in various research fields. In the field food research, protein are interesting candidates as functional ingredients. It essential to understand formation and properties for successful application products. This paper describes impact recent on general view process fibril from β-lg that formed, leading better control applications fibrils. There a need understanding behavior more complex systems.

参考文章(86)
Masao Doi, Sam F Edwards, The theory of polymer dynamics Oxford University Press. ,(1986)
Walraj S. Gosal, Allan H. Clark, Paul D. A. Pudney, Simon B. Ross-Murphy, Novel Amyloid Fibrillar Networks Derived from a Globular Protein: β-Lactoglobulin† Langmuir. ,vol. 18, pp. 7174- 7181 ,(2002) , 10.1021/LA025531A
Erica Frare, Patrizia Polverino de Laureto, Jesús Zurdo, Christopher M Dobson, Angelo Fontana, A Highly Amyloidogenic Region of Hen Lysozyme Journal of Molecular Biology. ,vol. 340, pp. 1153- 1165 ,(2004) , 10.1016/J.JMB.2004.05.056
Christopher M. Dobson, Protein folding and misfolding Nature. ,vol. 426, pp. 884- 890 ,(2003) , 10.1038/NATURE02261
Jean D. Sipe, Alan S. Cohen, Review: History of the Amyloid Fibril Journal of Structural Biology. ,vol. 130, pp. 88- 98 ,(2000) , 10.1006/JSBI.2000.4221
Geoffrey W. Smithers, Whey and whey proteins—From ‘gutter-to-gold’ International Dairy Journal. ,vol. 18, pp. 695- 704 ,(2008) , 10.1016/J.IDAIRYJ.2008.03.008
Salman S. Rogers, Paul Venema, Leonard M. C. Sagis, Erik van der Linden, Athene M. Donald, Measuring the Length Distribution of a Fibril System: A Flow Birefringence Technique Applied to Amyloid Fibrils Macromolecules. ,vol. 38, pp. 2948- 2958 ,(2005) , 10.1021/MA0474224
Luben N. Arnaudov, Renko de Vries, Theoretical modeling of the kinetics of fibrilar aggregation of bovine β-lactoglobulin at pH 2 Journal of Chemical Physics. ,vol. 126, pp. 145106- 145106 ,(2007) , 10.1063/1.2717159