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On the complexation of whey proteins

Delboni, Lariani A (author)
Lund University,Lunds universitet,Beräkningskemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Computational Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,University of São Paulo
Da Silva, Fernando Luis Barroso (author)
Lund University,Lunds universitet,Beräkningskemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Computational Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,University of São Paulo
 (creator_code:org_t)
Elsevier BV, 2016
2016
English.
In: Food Hydrocolloids. - : Elsevier BV. - 0268-005X. ; 55, s. 89-99
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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 alpha-lactalbumin, beta-lactoglobulin and lactoferrin were investigated by means of Monte Carlo simulations. The comparison between the free energies associated with the complexation of alpha-lactalbumine-lactoferrin and beta-lactoglobuline-lactoferrin at different pH and ionic strengths let us to explain why is experimentally observed the later complex and not the alpha-lactalbumine-lactoferrin complex. (C) 2015 Elsevier Ltd. All rights reserved.

Subject headings

NATURVETENSKAP  -- Kemi -- Teoretisk kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences -- Theoretical Chemistry (hsv//eng)

Keyword

Milk proteins
Electrostatic interactions
pH
Ionic strength
Molecular
modeling
Heteroprotein association

Publication and Content Type

art (subject category)
ref (subject category)

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