Method for preparing an enzymatic hydrolysate

Food or edible material: processes – compositions – and products – Fermentation processes

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426 18, 426 32, 426 34, 426 44, 426 49, 426656, 426657, 435 681, 435212, A23L 100

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053566378

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BRIEF SUMMARY
BACKGROUND OF THE INVENTION

The invention relates to a method for preparing an enzymatic hydrolysate containing di- and tripeptides, from a protein mixture, using proteolytic enzymes.
The subject of the present invention is also a di- and tripeptide-rich hydrolysate.
The importance of hydrolysates rich in di- and tripeptides and having a low free amino acid content is widely recognised by numerous scientific studies.
The physiological importance of the intestinal absorption of di- and tripeptides was discovered about thirteen years ago. Thus, the existence of intestinal transport systems for small peptides, different from those for free amino acids, and the greater efficacy of the absorption when the food supply of proteins is achieved from mixtures enriched with small peptides, have been demonstrated by SLEISENGER et al. in an article entitled "Evidence for a single common carrier for uptake of a dipeptide and tripeptide by hamster jejunum in vitro" published in the journal "Gastroenterology", volume 71, pages 76 to 81 (1976).
Compositions rich in di- and tripeptides are of real interest in dietetics not only for the nutrition of infants, convalescents and anaemic individuals, but also for that of patients whose intestinal absorption is altered, such as patients suffering from HARTNUP disease or cystinuria.
Both in individuals suffering from HARTNUP disease and in those suffering from cystinuria, amino acids are normally absorbed by the intestinal mucosa if they are present in dipeptide form (see BRINSON, R. R., HANUMANTHU, S. K., and PITTS, W. M. (1989): "A reappraisal of the peptide based enteral formulas: clinical applications", Nutritional in Clinical Practice 4:211-217; NAYAB, F. and ASATOOR, A. M. (1970): "Studies on intestinal absorption of amino acids and a dipeptide in a case of Hartnup disease", Gut (Journal of the British Society for Gastroentology) volume 11, pages 373-379 (1970)).
Consequently, the invention can for example be applied in hospital diets, in particular in artificial nutrition administered orally, enterally or parenterally, more particularly by intravenous infusion.
Artificial nutrition is essential for patients incapable of normal feeding because of an incapacity due to a physical damage caused by an accident, a surgical operation, an oesophageal trauma or because of a general physiological state which does not permit normal feeding, (coma, burns).
Other possible applications are immunostimulation or animal nutrition, particularly fish feed, or use as growth stimulator.
Various methods are known for preparing protein hydrolysates containing di- and tripeptides: alkaline or acid hydrolysis, enzymatic hydrolysis and chemical synthesis. However, all of these known methods do not enable a hydrolysate containing not less than 75 mole % di- and tripeptides to be prepared from animal and/or vegetable proteins.
Proteins which can be used for manufacturing a hydrolysate on an industrial scale are, by way of example, as follows:
egg proteins (ovalbumin);
milk proteins: casein, whey, lactalbumins, lactoglobulins;
slaughtering blood proteins: blood plasma, serum albumin, decolorised haemoglobin;
products from the fishing and fish-canning industries, and
proteins of plant origin: soybean and lucerne proteins.
Alkaline hydrolysis or acid hydrolysis of mixtures of proteins such as lactalbumin, ovalbumin, whey and casein by means of strong acids or bases is used at high temperature so as to break the chemical bonds. It leads to the production of mixtures which are greatly enriched in free amino acids and often very highly contaminated with salts (Cl.sup.-, Na.sup.+) which are difficult to remove.
The known chemical methods are easy to implement and enable high levels of hydrolysis to be obtained by breaking a large number of peptide bonds. However, they are drastic and cause the formation of undesirable side reactions as well as a decrease in the nutritional value of the proteins through the degradation of essential amino acids.
Thus, alkaline hydrolysis at high temperature (100 .degree. to 1

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