By Steve Taylor
ISBN-10: 0120164477
ISBN-13: 9780120164479
Advances in meals and nutrients acknowledges the fundamental dating among the meals and dietary sciences and brings jointly notable and accomplished reports that spotlight this courting. Contributions element the medical advancements within the huge parts of nutrition technological know-how and meals are meant to make sure that nutrition scientists in academia and in addition to specialist nutritionists and dieticians are stored knowledgeable touching on rising study and advancements in those vital disciplines.
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Extra resources for Advances in Food and Nutrition Research, Vol. 47
Sample text
As estimated by the particle sizes, the maximum emulsifying capacity was obtained from hydrolysates with a 10 or 20% DH. Higher hydrolysis resulted in peptides that were too short to act as effective emulsifiers, and, at lower proteolysis, the somewhat reduced solubility of the hydrolysates slightly decreased their emulsifying power. All the emulsions were unstable when they were subjected to heat treatment at high temperatures (1228C for 15 min), but emulsions prepared from the less hydrolyzed peptide mixtures were stable to heat treatment at 908C for 30 min.
Secondary proteolysis during cheese ripening. The ACEinhibitory activity in cheese was mainly associated with the low molecular mass peptide fraction. 3. Peptides with immunomodulatory activities The bioactivity of immunopeptides has been characterized by different in vitro and in vivo test systems. Casein-derived immunopeptides including fragments of aS1- and b-casein (Table V) have been shown to stimulate phagocytosis by murine macrophages, and to exert a protective effect against MILK PROTEIN TAILORING 49 Klebsiella pneumoniae infection in mice after intravenous treatment (Meisel and Schlimme, 1996).
CHOBERT interactions, is often stabilized by intra- and intermolecular bonds. , 1994). The capacity and rate by which whey proteins aggregate is controlled by factors such as protein concentration, pH, temperature and presence of other components. According to Aguilera (1995), aggregation can take place in three steps: denaturation, aggregation, and gelification. Aggregation is more rapid near the isoelectric point of proteins. For a review on the effect of thermal treatment on milk protein structure, see Cayot and Lorient (1998).
Advances in Food and Nutrition Research, Vol. 47 by Steve Taylor
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