Casein hydrolysate. III. Some functional properties of hydrophobic peptides synthesized from hydrolysate

Two different kinds of ‘plastein type’ peptide preparations, one dispersible (yield 97%, w/w of total casein) and the other indispersible (yield 3% w/w of total casein) in water, were synthesized by treating casein hydrolysate with papain. These preparations gave similar elusion patterns by reverse...

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Bibliographic Details
Published inFood hydrocolloids Vol. 5; no. 6; pp. 573 - 579
Main Authors Mozaffar, Zahid, Haque, Zahur U.
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 01.02.1992
Elsevier
Subjects
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Biological and medical sciences
Biotechnology
Food industries
Fundamental and applied biological sciences. Psychology
Hydrolysis
Casein
Peptides
Enzyme
Gel electrophoresis
HPLC chromatography
Papain
Hydrophobicity
Immobilized enzyme
Physicochemical properties
Thermal stability
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Summary:Two different kinds of ‘plastein type’ peptide preparations, one dispersible (yield 97%, w/w of total casein) and the other indispersible (yield 3% w/w of total casein) in water, were synthesized by treating casein hydrolysate with papain. These preparations gave similar elusion patterns by reverse phase high performance liquid chromatography (HPLC) and gave large aggregates with electrophoretic mobility, comparable to that of non-modified casein by non-SDS—PAGE. These aggregates were dissociated by sodium dodecyl sulfate (SDS), indicating non-covalent interaction. Oil holding capacity of both peptide preparations was significantly improved compared to casein or its hydrolysate. The dispersible peptide preparation was highly soluble at neutral pH and was more thermostable than casein. Emulsion activity and stability of both preparations were decreased.
ISSN:0268-005X
1873-7137
DOI:10.1016/S0268-005X(09)80126-4