Whey Proteins and Peptides in Human Health

Author(s):  
P. E. Morris ◽  
R. J. Fitzgerald
Therapy ◽  
2006 ◽  
Vol 3 (1) ◽  
pp. 69-78 ◽  
Author(s):  
Josée Beaulieu ◽  
Claude Dupont ◽  
Pierre Lemieux

2000 ◽  
Vol 84 (S1) ◽  
pp. 91-98 ◽  
Author(s):  
Gerd E. Vegarud ◽  
T. Langsrud ◽  
C. Svenning

Minerals and trace elements in cow's milk occur as inorganic ions and salts or form complexes with proteins and peptides, carbohydrates, fats and small molecules. The main mineral binder or chelators of calcium are the caseins, αs1-casein, αs2-casein, β-casein and κ-casein, but also whey proteins and lactoferrin bind specific minerals like calcium, magnesium, zinc, iron, sodium and potassium. Less documented is the binding of trace elements. Peptides obtained byin vitroorin vivohydrolysis act as mineral trappers through specific and non-specific binding sites. They may then function as carriers, chelators, of various minerals and thus enhance or inhibit bioavailability. Peptides from milk proteins have found interesting new applications in the food industry as products with improved functionality or as ingredients of dietary products, or used in pharmaceutical industry. Fortification of foods with minerals in a low concentration has for a long time been used in some countries to overcome mineral deficiency, which is an increasing problem in humans. These types of foods are being used to create a new generation of super foods in the industry today.


2008 ◽  
Vol 26 (No. 1) ◽  
pp. 15-23 ◽  
Author(s):  
B. Wróblewska ◽  
L. Jędrychowski ◽  
G. Hajós ◽  
E. Szabó

The aim of the research was to determine the changes in the immunoreactivity of whey protein concentrate (WPC) modified by two enzymes: proteinase, Alcalase 2.4L FG (Novo Nordisk), and cross-linked transglutaminase (EC 2.3.2.13, Activa<sup>TM</sup> P, m-TG, Ajinomoto). The new products were characterised by 2D electrophoresis, immunoblotting, and ELISA methods. The WPC hydrolysate obtained with Alcalase contained proteins and peptides characterised mostly by low molecular weight peptides (MW < 14.4 kDa) in the pH range of 3–10. Immunoblotting showed strong immunoreactive properties of the hydrolysate with &alpha;-la and &beta;-lg polyclonal rabbit antibodies. The 2D electrophoretic patterns of WPC and its modified product obtained with m-TG did no differ significantly. However, the immunoblot analysis demonstrated that WPC showed a stronger reactivity towards IgE of allergic patients as compared to WPC with m-TG. ELISA methods showed that two-step hydrolysis with Alcalase followed by m-TG significantly reduced the immunoreactive properties of whey proteins. No cross reactions were observed with α-la and only about 0.6% cross-reactivity with &beta;-lg.


Nutrafoods ◽  
2011 ◽  
Vol 10 (2-3) ◽  
pp. 29-42 ◽  
Author(s):  
Anne Pihlanto

Author(s):  
K. Petrotos ◽  
E. Tsakali ◽  
P. Goulas ◽  
A.G. D'Alessandro
Keyword(s):  

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