TY - JOUR
T1 - Reconstituted micelle formation using reduced, carboxymethylated bovine κ-casein and human β-casein
AU - Sood, Satish M.
AU - Lekic, Tim
AU - Jhawar, Harbir
AU - Farrell, Harold M.
AU - Slattery, Charles W.
N1 - In milk, kappa-casein, a mixture of disulfide-bonded polymers, stabilizes and regulates the size of the unique colloidal complex of protein, Ca2+ and inorganic phosphate (Pi) termed the casein (CN) micelle. However, reduced, carboxymethylated bovine kappa-CN (RCM-kappa) forms fibrils at 37 degrees C and its micelle-forming ability is in question.
PY - 2006/7
Y1 - 2006/7
N2 - In milk, κ-casein, a mixture of disulfide-bonded polymers, stabilizes and regulates the size of the unique colloidal complex of protein, Ca 2+ and inorganic phosphate (Pi) termed the casein (CN) micelle. However, reduced, carboxymethylated bovine κ-CN (RCM-κ) forms fibrils at 37°C and its micelle-forming ability is in question. Here, the doubly- and quadruply-phosphorylated human β-CN forms and 1:1 (wt:wt) mixtures were combined with RCM-κ at different β/κ weight ratios. Turbidity (OD400 nm) and a lack of precipitation up to 37°C were used as an index of micelle formation. Studies were with 0, 5 and 10 mM Ca2+ and 4 and 8 mM Pi. The RCM-κ does form concentration-dependent micelles. Also, β-CN phosphorylation level influences micelle formation. Complexes were low-temperature reversible and RCM-κ fibrils were seen. There appears to be equilibrium between fibrillar and soluble forms since the solution still stabilized after fibril removal. The RCM-κ stabilized better than native bovine κ-CN.
AB - In milk, κ-casein, a mixture of disulfide-bonded polymers, stabilizes and regulates the size of the unique colloidal complex of protein, Ca 2+ and inorganic phosphate (Pi) termed the casein (CN) micelle. However, reduced, carboxymethylated bovine κ-CN (RCM-κ) forms fibrils at 37°C and its micelle-forming ability is in question. Here, the doubly- and quadruply-phosphorylated human β-CN forms and 1:1 (wt:wt) mixtures were combined with RCM-κ at different β/κ weight ratios. Turbidity (OD400 nm) and a lack of precipitation up to 37°C were used as an index of micelle formation. Studies were with 0, 5 and 10 mM Ca2+ and 4 and 8 mM Pi. The RCM-κ does form concentration-dependent micelles. Also, β-CN phosphorylation level influences micelle formation. Complexes were low-temperature reversible and RCM-κ fibrils were seen. There appears to be equilibrium between fibrillar and soluble forms since the solution still stabilized after fibril removal. The RCM-κ stabilized better than native bovine κ-CN.
KW - Amyloid fibrils
KW - Colloidal calcium phosphate
KW - Human β-caseins
KW - Reconstituted milk micelle formation
KW - Reduced, carboxymethylated κ-casein
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U2 - 10.1007/s10930-006-9022-7
DO - 10.1007/s10930-006-9022-7
M3 - Article
C2 - 16947075
SN - 1572-3887
VL - 25
SP - 352
EP - 360
JO - Protein Journal
JF - Protein Journal
IS - 5
ER -