Department of Dairy Chemistry, Dairy Science College, Karnataka Veterinary, Animal & Fisheries Sciences University, Bangalore-560 024
*Corresponding Author: Nagamani. A, #16, Kalpavruksha Ladies Hostel, Hebbal, Bangalore-560 024, Karnataka (State), India. Email: nagudscb@gmail.com
Online published on 5 September, 2012.
Skim milk subjected to acidification by the addition of 10% HCl to separate whole casein at 5% degree of hydrolysis for about 3 hr. Casein hydrolysates produced by neutrase and trypsin yielded 75% of hydrophobic and 83.3% relatively hydrophilic CPPs respectively. The CPPs showed calcium binding ability of 0.40 and 0.45 mg of Ca/mg of the CPPs obtained from hydrophobic and relatively hydrophilic CPPs respectively. With statistical significant difference (P≥0.05). The solubilizing ability of CPPs of 11.92 and 11.56 mg of Ca/mg of CPPs were observed at 12mg of Ca/mg of CPPs obtained from hydrophobic and relatively hydrophilic CPPs respectively.
Caseinophosphopeptides, Calcium binding, Calcium Solubilizing, Hydrophobic, Hydrophilic
