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  • Author or Editor: M. Silvestre x
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With a view to increasing the industrial use of bovine blood globin, the extraction of the globin fraction was achieved using the acidified acetone method. Spectrophotometric analysis of the globin and the extracted heme group was performed utilizing the Soret band. The influence of the type of final processing of the globins (freeze drying, gel) on the solubility, the emulsification capacity, the emulsifying activity index and the stability of the emulsion was studied at pH 5, 6 and 7. No behavioural differences between freeze-dried and gel globin forms were observed. The best performance for most of the functional properties was achieved at pH 5.0 for the globin obtained by this method.

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Hydrolytic parameters were tested to prepare casein hydrolysates with high oligopeptide content for dietetic purpose, using papain. Employing a temperature of 37 °C and an E:S ratio of 2% was the most economical condition for large-scale manufacture. The encapsulation in liposomes was used for masking the bitterness, and was also able to reduce the hydrophobicity as well as to keep the chemical stability during 60 days of storage. The UV spectrometry with second derivative transformation was used to measure the encapsulation rate, which changed from 56% to 62%. The size distribution of vesicles was in the range of 500 to 1000 nm.

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