Papain hydrolysates of casein: molecular weight profile and encapsulation in lipospheres

Some reaction parameters were tested in the hydrolysis of casein by papain, in order to prepare hydrolysates with high oligopeptide contents, for either dietetic or pharmaceutical purposes. Five casein hydrolysates were prepared and then fractionated by size-exclusion HPLC. The rapid correct fractio...

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Bibliographic Details
Published in:	Journal of the science of food and agriculture Vol. 84; no. 14; pp. 1891 - 1900
Main Authors:	Barbosa, C.M.S, Morais, H.A, Delvivo, F.M, Mansur, H.S, Oliveira, M.C. de, Silvestre, M.P.C
Format:	Journal Article
Language:	English
Published:	Chichester, UK John Wiley & Sons, Ltd 01-11-2004 Wiley John Wiley and Sons, Limited
Subjects:	Biological and medical sciences bitterness casein casein hydrolysates Chemical products encapsulation Enzymes Food industries Food science Fundamental and applied biological sciences. Psychology lipospheres Milk and cheese industries. Ice creams molecular weight oligopeptides papain peptide profile Peptides Proteins proteolysis Taste Encapsulation Peptides Enzyme Cysteine endopeptidases lipospheres Papain Profile Peptidases Milk protein Casein Hydrolysate bitterness peptide profile Hydrolases Molecular mass casein hydrolysates
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Summary:	Some reaction parameters were tested in the hydrolysis of casein by papain, in order to prepare hydrolysates with high oligopeptide contents, for either dietetic or pharmaceutical purposes. Five casein hydrolysates were prepared and then fractionated by size-exclusion HPLC. The rapid correct fraction area method was used for quantifying peptides and free amino acids. Among the five reaction conditions tested, three produced similar peptide profiles. However, the use of a temperature of 37°C and an E:S ratio of 2% is probably the most economical condition for use in large-scale manufacture. With the aim of masking the bitterness of these preparations, a new method, based on the encapsulation in lipospheres, was used. Also, second derivative spectrophotometry was used for the first time to measure the extent of encapsulation of protein hydrolysates, which changed from 50% to 83%. Moreover, the efficiency of this system was evaluated by analysing other parameters, which showed a reduction of hydrophobicity and bitterness of all samples, as well as good chemical stability during 60 days of storage under refrigeration. The electron microscopical analysis of liposheres showed an average size around 5.0 ± 1.0 micrometer.
Bibliography:	ArticleID:JSFA1855 CNPq istex:6EBE0E7A1C8081BA2ACC176F7B4961657C251387 FAPEMIG ark:/67375/WNG-TQH5G0XR-6 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23
ISSN:	0022-5142 1097-0010
DOI:	10.1002/jsfa.1855