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Protein hydrolysate rich in tripeptides

a tripeptide and protein hydrolysate technology, applied in the field of protein hydrolysate, can solve the problems of residual immunogenic materials, low yield of nutritionally indispensible amino acids, and bitter tas

Inactive Publication Date: 2005-11-17
DSM IP ASSETS BV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Unfortunately the hydrolysis process required to realise these benefits comes with a number of disadvantages.
These include bitter off-tastes, residual immunogenic materials, low yields of nutritionally indispensible amino acids, high osmotic values caused by the release of free amino acids and, finally, limited acid stabilities.
Unfortunately these enzyme combinations always yield peptide mixtures which are bitter and exhibit a broad molecular weight distribution.
Large molecular weight peptides are undesirable because they are responsible for the allergenic response and their uptake requires additional enzymatic processing steps in the intestine.
Disadvantages of this debittering process are the release of substantial quantities of free amino acids and thus brothy off flavors and losses of nutritionally important amino acids.
In conclusion, industrial production of protein hydrolysates continues to rely on enzyme mixtures which are far from optimal so that expensive purification steps are needed to produce peptide mixtures having sub-optimal size distributions.

Method used

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  • Protein hydrolysate rich in tripeptides
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Examples

Experimental program
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Effect test

example 1

Properties of the Tripeptidylpeptidase Encoded by Gene 12 (TPAP-A) of Aspergillus niger

[0077] The enzyme encoded by gene 12 (described in our copending application PCT / EP02 / 01984) was overproduced in an A. niger host cell and chromatographically purified. Purification was carried out on a Resource Q column in 50 millimol / liter acetate pH 4.5. Elution by increasing the NaCl concentration yielded the enzyme in a sharp activity peak. Activity was measured by incubation with the synthetic peptide Ala-Ala-Phe-pNA. The solution with the purified enzyme contained 8 units / ml if tested on the synthetic tripeptide Ala-Ala-Phe-pNA at pH 4.0 and 60 degrees C. (see Materials & Methods section).

[0078] In a first experiment, the pure enzyme was incubated at pH 5 and 50 degrees C. with two different synthetic chromogenic substrates i.e. Ala-Ala-Phe-pNA and Ala-Phe-pNA (both from Bachem, Switserland). Stock solutions of these peptides were made in DMSO which were then diluted 100× in the desired a...

example 2

Casein hydrolysates subjected to a proline-specific endoprotease in combination with a tripeptidylaminopeptidase are non-bitter and contain a high proportion of tripeptides having carboxyterminal proline residues.

[0083] A 6% (w / w on protein) casein solution was prepared by dissolving sodium caseinate in water. After adjustment of the pH to 8.0 by NaOH, the serine protease Delvolase was added to a concentration of 4% (volume of the commercial enzyme product per weight of sodium caseinate) and the mixture was incubated for 2.5 hours at 60 degrees C. under non-pH-stat conditions. Then the reaction was stopped by lowering the pH to 5.0 using lactic acid followed by a heat treatment of 10 minutes at 90 degrees C. The solution was cooled down to 50 degrees C. and two samples were taken. The first sample (Sample A) served as a reference characterizing the material that has been subjected to the action of a broad spectrum serine protease only. The second sample was used for subsequent incu...

example 3

Frequency of Di- and Tripeptides Having Carboxyterminal Proline Residues in a Commercial Casein Based Infant Formula Product

[0088] Among the various infant formula products tested (see Example 6 in our copending application PCT / EP01 / 14480) Nutramigen (Mead Johnson, containing 14 grams of casein hydrolysate per 100 gram powder) contains the highest (i.e. 22%) molar fraction of peptides carrying C-terminal proline. In the present Example we show the results of a LC / MS analysis of this hydrolysate with a focus on its content in di and tripeptides and the frequency of such peptides having carboxyterminal proline residues.

[0089] Prior to LC / MS analysis the fatty material present in infant formulae had to be removed. As specified in the Materials & Methods section this was carried out by a hexane extraction. The aqueous phase thus obtained was centrifuged, filtered and then subjected to LC / MS analysis to characterize the various peptides present.

[0090] According to the results obtained...

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Abstract

The present invention describes a protein hydrolysate which is rich in tripeptides whereby the tripeptides are rich in proline at one end of the peptide.

Description

FIELD OF THE INVENTION [0001] The present invention relates to protein hydrolysate and the uses thereof. BACKGROUND OF THE INVENTION [0002] There is increasing interest in the use of protein hydrolysates for both medical and non-medical applications. In both applications an easily assimilable diet featuring facilitated gastrointestinal uptake of proteins is a factor of prime importance. Protein hydrolysates for medical applications also require strongly reduced allergenic properties. For products intended for non-medical applications, good taste characteristics and good solubilities under acid conditions are important characteristics. Unfortunately the hydrolysis process required to realise these benefits comes with a number of disadvantages. These include bitter off-tastes, residual immunogenic materials, low yields of nutritionally indispensible amino acids, high osmotic values caused by the release of free amino acids and, finally, limited acid stabilities. [0003] In prior public...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A23J3/10A23J3/34A23L1/30A23K1/165A23L1/305A61K38/00A61K38/17C07K5/00C12N9/48C12N15/57C12P21/06
CPCC12N9/48
Inventor EDENS, LUPPODEKKER, PETRUS JACOBUS THEODORUSROOS DE, ANDRE LEONARDUS
Owner DSM IP ASSETS BV
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