Process for Preparation of Packaged Heat-Preserved Aqueous Drink Comprising Casein Micelles and Tryptophan-Rich Peptides, and Products so obtained

a technology of tryptophan and peptides, which is applied in the field of process, can solve the problems of low tryptophan level taken up by the brain, difficult to approach milk or milk-like drinks, and difficult to observe significant effects, etc., and achieves the effect of high blood plasma tryptophan/lnaa ratio

Inactive Publication Date: 2009-10-29
CONOPCO INC D B A UNILEVER
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0027]The tryptophan-comprising peptide composition which is preferably used in the RTD formulation according to the present invention is preferably a lysozyme hydrolysate or a purified lysozyme hydrolysate. Preferably, said lysozyme hydrolysate is particularly rich in arginine residues. Arginine does not belong to the group large, neutral amino acids (LNAA's) but is known for its insulin stimulating effect. It has been found that the hydrolysate as herein disclosed can generate in vivo high blood plasma tryptophan / LNAA ratios. The tryptophan / LNAA ratios detected in blood plasma, were found to be higher than the tryptophan / LNAA ratio of the hydrolysate. Yet another advantage of the tryptophan-containing peptide composition herein described is that the tryptophan-containing peptides are very small so that even in combination with protein-rich products with less favorable tryptophan / LNAA ratios, the hydrolysate can immediately generate high blood plasma tryptophan / LNAA ratios. This thus makes such tryptophan-containing peptide composition well suitable in the RTD formulations of the present invention. The tryptophan-containing peptide composition as used in the RTD formulation of the present invention may further comprise free tryptophan. Preferably the hydrolysate of the tryptophan-containing peptide composition does not contain more than 1 wt % (on dry matter) of free tryptophan.

Problems solved by technology

However, tryptophan is not the only amino acid taken up, and in fact when an average animal protein composition is ingested, the level of tryptophan taken up by the brain is so low due to competitive uptake of other amino acids that usually no significant effect can be observed attributable to tryptophan.
Use of tryptophan as free amino acids has disadvantages, in that food legislation in many countries limits the use of tryptophan as free amino acid in foodstuffs.
Whilst colour and flavour can be made up by colourants and / or flavouring agents (and such is quite common for milk-like health drinks aimed at children, like flavouring with chocolate, banana or strawberry), the mouthfeel of milk or milk-like drinks is a bit more difficult to approach.

Method used

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Examples

Experimental program
Comparison scheme
Effect test

example 1

[0077]Hydrolyzing Lysozyme using Protex and Identity of the Peptides Formed.

[0078]A solution containing 10% (w / w) pure lysozyme was adjusted to pH 8.2 using NaOH and heated to 52 degrees C. Hydrolysis was started by adding 25 microliter of Protex / g of protein present. Under continuous stirring and maintaining the pH at 8.2, the hydrolysis was continued for 5.5 hours to yield an almost clear solution without a visible precipitate. After a heating step to inactivate the Protex activity, a sample was taken for DH analysis. The DH of the solution turned out to be almost 30%. The heat treated solution was ultrafiltered over a 10 kDa filter to yield a completely clear liquid. This clear liquid was used for LC / MS analysis, for molecular weight distribution of peptides and proteins present as well as for ion exchange chromatography.

[0079]To get an impression of the molecular weight distribution of peptides and proteins present, the clear liquid was subjected to a molecular size analysis as ...

example 2

[0082]Increasing the Tryptophan Content of the Hydrolysate

[0083]Lysozyme incorporates a surprising high amount of the basic arginine and lysine residues. Furthermore the lysozyme molecule incorporates a significant number of the acid glutamate and aspartate residues. This data has been used to devise an innovative and elegant purification route towards hydrolysates featuring high tryptophan / LNAA ratios. Essential requirement for this purification route is, however, that only very few of the tryptophan residues show up in peptides also containing either an arginine or lysine residue or a glutamate or aspartate residue. As shown in Example 1, the specific hydrolysis route used here yields only few tryptophan containing peptides containing an arginine residue and no peptides containing a lysine, glutamate or aspartate residue.

[0084]Theory predicts that a maximal charge difference between peptides with and without a glutamate or aspartate residue can be achieved around pH 3. A maximal c...

example 3

Large Scale Lysozyme Hydrolysis

[0087]In larger scale lysozyme hydrolysis procedures, essentially the procedure as described in Example 1 was followed with some minor modifications. A solution containing 7.3% (w / w) pure lysozyme was heated to 65 degrees C. after which the pH was adjusted to pH 8.2 using NaOH. Hydrolysis was started by adding 25 microliter of Protex 6 L / g dry matter. Under continuous stirring and maintaining the pH at 8.2 and the temperature at 53 degrees C., the hydrolysis was continued for 2 hours. Then the pH value was increased to 9.0 and incubation was pursued for another 3.5 hours to yield a solution with some precipitate. Then the pH of the solution was lowered to 4.5 and the solution was cooled to below 4 degrees C. To obtain a completely clear product, the liquid was filtered over a Z 2000 filter (Pall) and subsequently excess water and salt was removed via nanofiltration. The resulting concentrate was then subjected to an UHT treatment of 7 seconds at 120 de...

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PUM

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Abstract

A process to prepare packaged pasteurized or sterilized aqueous drinkable products which comprise casein micelles (e.g. from dairy protein) and peptide-fractions, which peptide fractions are rich in tryptophan, and the products so-obtained. The process requires a heat preservation at a specific pH.

Description

FIELD OF THE INVENTION [0001]The present invention relates to a process to prepare packaged heat-preserved (e.g. pasteurized or sterilized) aqueous drinkable products which comprise casein micelles (e.g. from dairy products) and peptide-fractions, which peptide fractions are rich in tryptophan, and the products so-obtained.BACKGROUND OF THE INVENTION [0002]Recently, there have been various reports on the benefit which tryptophan is believed to have on several aspects of human behaviour, mood, brain function, brain development, when such tryptophan is taken up by the brain. Examples of such reports are WO 99 / 55174, WO 00 / 42868, WO 2005 / 023017.[0003]Tryptophan is an amino acid present in many proteins, like e.g. whey proteins, but also animal protein contains tryptophan. Tryptophan can be taken up in the blood, and from the blood into the brain, after ingestion of a protein which contains tryptophan. However, tryptophan is not the only amino acid taken up, and in fact when an average ...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A23C3/02A23C9/20B65D85/80A23C9/154
CPCA23C9/1526A23C11/08A23L1/3053A23L1/3056A23L2/52A23V2002/00A23L2/66A23V2250/54246A23V2250/065A23L33/18A23L33/19A23C9/152
Inventor VAN BECKHOVEN, RUDOLF FRANCISCUS W C.BOT, ARJENDUCHATEAU, ALEXANDER LUCIA L.EDENS, LUPPOKLOEK, JORISDE ROOS, ANDRE LEONARDUS
Owner CONOPCO INC D B A UNILEVER
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