کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
603657 | 1454422 | 2016 | 11 صفحه PDF | دانلود رایگان |
• Simplified computer models can aid the understanding of mechanisms in food science.
• Whey proteins were designed to have their optimal attractive features at pH 6.
• No association is expected for the system α-LA and β-LG.
• The free energy of interaction between α-LA and LF revealed a weak at-traction.
• Protein charge-charge plays a key role in the studied systems.
Milk proteins have a rich diversity of physical chemistry and biodegradable properties which makes them appealing for different food and pharmaceutical applications. Theoretical coarse grained models and numerical simulations were employed here in order to gain novel insight into the understanding of the fundamental mechanisms of the process of milk proteins complexation in a diversity of environmental conditions. The interactions between α-lactalbumin, β-lactoglobulin and lactoferrin were investigated by means of Monte Carlo simulations. The comparison between the free energies associated with the complexation of α-lactalbumin–lactoferrin and β-lactoglobulin–lactoferrin at different pH and ionic strengths let us to explain why is experimentally observed the later complex and not the α-lactalbumin–lactoferrin complex.
Figure optionsDownload as PowerPoint slide
Journal: Food Hydrocolloids - Volume 55, April 2016, Pages 89–99