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Process optimisation for preparation of caseinophosphopeptides from Buffalo milk casein and their characterisation

Published online by Cambridge University Press:  23 July 2014

Prerna Saini ,
Bimlesh Mann ,
Rajesh Kumar ,
Rajan Sharma ,
Ram Ran Bijoy Singh  and
Alok Chatterjee
Prerna Saini
Affiliation:
Dairy Chemistry Division, National Dairy Research Institute, Karnal-132001, India
Bimlesh Mann*
Affiliation:
Dairy Chemistry Division, National Dairy Research Institute, Karnal-132001, India
Rajesh Kumar
Affiliation:
Dairy Chemistry Division, National Dairy Research Institute, Karnal-132001, India
Rajan Sharma
Affiliation:
Dairy Chemistry Division, National Dairy Research Institute, Karnal-132001, India
Ram Ran Bijoy Singh
Affiliation:
Division of Dairy Technology, National Dairy Research Institute, Karnal-132001, India
Alok Chatterjee
Affiliation:
Division of Dairy Technology, National Dairy Research Institute, Karnal-132001, India
*
*For correspondence; e-mail: bimleshmann@gmail.com
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Abstract

Caseinophosphopeptides (CPPs) are multifunctional bioactive peptides containing phosphorylated seryl residues in their sequence. In the present study, method for the production of CPPs from buffalo milk casein was optimised and characterised for their sequence, calcium solubilising and calcium binding activities. Response surface methodology was used to optimise the conditions for hydrolysis of buffalo casein by trypsin to obtain maximum yield of CPPs. The optimum hydrolysis conditions were as follows: hydrolysis pH 7·5, temperature 37 °C, hydrolysis time 7·0 h. Under these conditions, the experimental yield obtained was 10·04±0·24%, which is slightly lower than value predicted by the model. These CPPs were able to solubilise 1·03±0·08 mg la/mg CPPs in presence of excess phosphate and bind 0·935 mg of Ca/mg of CPPs. Eight phosphopeptides i.e. αs1-CN f (37-58) 2P; αs1-CN f (37-58) 3P; αs1-CN f (35-58) 2P; αs1-CN f (35-58) 3P; αs2-CN f (2-21) 4P; αs2-CN f (138-149) 1P; β-CN f (2-28) 4P and β-CN f (33-48) 1P were identified by LC-MS/MS which contained motif for binding of divalent minerals. The sequences of these CPPs differed from that of derived from bovine casein.

Keywords

Caseinophosphopeptidescalcium binding ability and Buffalo milk
Type
Research Article
Information
Journal of Dairy Research , Volume 81 , Issue 3 , August 2014 , pp. 364 - 371
Copyright
Copyright © Proprietors of Journal of Dairy Research 2014 

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