Peptides From Milk Proteins and Their Properties

Arun Kilara, Dinakar Panyam

Research output: Contribution to journalReview article

168 Citations (Scopus)

Abstract

The physico-chemical properties of food proteins such as hydrophilicity, hydrophobicity and intermolecular interactions are influenced by intrinsic nature of proteins. The controlled enzymatic modification of casein and whey proteins by proteolysis generates total hydrolyzate. The total hydrolyzate is fractionated to low molecular weight peptides and high molecular weight materials. Solubility is essential prerequisite for functional properties manifestation and enzyme hydrolysis enables solubility of milk protein modeling techniques which determines structures in these peptides.

Original languageEnglish (US)
Pages (from-to)607-633
Number of pages27
JournalCritical reviews in food science and nutrition
Volume43
Issue number6
DOIs
StatePublished - Jan 1 2003

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Milk Proteins
milk proteins
Hydrophobic and Hydrophilic Interactions
Solubility
Peptides
solubility
Molecular Weight
peptides
molecular weight
Proteins
Caseins
whey protein
hydrophobicity
Molecular weight
dairy protein
proteolysis
Proteolysis
protein sources
functional properties
casein

All Science Journal Classification (ASJC) codes

  • Food Science
  • Industrial and Manufacturing Engineering

Cite this

Kilara, Arun ; Panyam, Dinakar. / Peptides From Milk Proteins and Their Properties. In: Critical reviews in food science and nutrition. 2003 ; Vol. 43, No. 6. pp. 607-633.
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Peptides From Milk Proteins and Their Properties. / Kilara, Arun; Panyam, Dinakar.

In: Critical reviews in food science and nutrition, Vol. 43, No. 6, 01.01.2003, p. 607-633.

Research output: Contribution to journalReview article

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