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Protein hydrolysates enriched in peptides having a carboxy terminal proline residue

A proline and amino acid technology, applied in the direction of protein food ingredients, hydrolytic enzymes, microorganisms, etc., can solve undesirable, bitter taste and other problems

Inactive Publication Date: 2007-05-02
DSM IP ASSETS BV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

According to JP5015314, the presence of a proline residue at the carboxy terminus of the peptide results in a bitter taste and is undesirable

Method used

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  • Protein hydrolysates enriched in peptides having a carboxy terminal proline residue
  • Protein hydrolysates enriched in peptides having a carboxy terminal proline residue

Examples

Experimental program
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Effect test

Embodiment 1

[0215] Hydrolysis of β-casein with subtilisin in combination with a proline-specific endoprotease from Chryseobacterium meningosepticum

[0216] β-casein represents a major casein component in milk. The protein is well characterized in terms of its amino acid sequence and is commercially available in nearly pure form. Likewise, β-casein provides an excellent assay substrate to study the relationship between cleavage sites and the lengths of the various peptides formed during enzymatic hydrolysis.

[0217] This example demonstrates that despite the broad spectrum profile of subtilisins, the addition of very specific enzymes such as proline-specific endoproteases can have a major effect on the size of the β-casein fragments formed. Improved yields of casein fractions can thus be obtained by incubation with subtilisin and proline-specific endoproteases. β-casein is relatively proline-rich, as acid hydrolysis and subsequent amino acid analysis in the Materials and Methods sectio...

Embodiment 2

[0222] Beta-Casein Hydrolyzate and Bitterness

[0223] Although Example 1 illustrates the effect of a proline-specific endoprotease on peptide size and the proportion of peptides with carboxy-terminal proline residues, the effect of this enzyme on bitter taste was not measured in Example 1. Casein hydrolysates are notoriously bitter and this property is related to their relatively high content of hydrophobic amino acid residues.

[0224] To examine the effect of proline-specific endoproteases on the taste of β-casein hydrolyzed by subtilisin, Delvolase was used as described in Example 1. TM and Delvolase TM Enzyme incubation with proline-specific endoprotease. After heat inactivation of both subtilisin and proline-specific endoprotease, samples were cooled to room temperature and distilled water was added to give a final casein concentration of 4% (w / w). The taste of the latter solution was then evaluated by a panel of experienced tasters. The taster unanimously concluded ...

Embodiment 3

[0227] Isolation of proline-specific endoprotease from Aspergillus niger

[0228] A large group of molds capable of forming black spores was grown on a medium containing 1.0 g K 2 HPO 4 , 0.5g KH 2 PO 4 , 0.5g KCl, 0.5g MgSO 4 .7H 2 O, 0.01g FeSO 4 .7H 2 O, 5 g glucose, 15 g collagen (Sigma) and distilled water were added to give a volume of 1 liter on pH 6.5 medium. The inoculum for each experiment was prepared by imbibing fungal spores (5 days old) grown on agar slants in 5 ml of sterile water. 2% (v / v) of the latter suspension was used for inoculation of pH 6.5 medium. It was grown with shaking at 28°C for 100 hours after which time the culture was filtered and a sample of the clear filtrate was incubated with the synthetic peptide Z-Ala-Pro-pNA (Bachem; Bubendorf, Switzerland) at pH 5.0 and 50°C. Samples capable of releasing pNA were identified by measuring the increase in absorbance at 410 nm. Further studies were performed on positive strains that produced rela...

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Abstract

The present invention provides An isolated polypeptide which has proline specific endoprotease activity, selected from the group consisting of:(a) a polypeptide which has an amino acid sequence which has at least 40% amino acid sequence identity with amino acids 1 to 526 of SEQ ID NO:2 or a fragment thereof;(b) a polypeptide which is encoded by a polynucleotide which hybridizes under low stringency conditions with (i) the nucleic acid sequence of SEQ ID NO:1 or a fragment thereof which is at least 80% or 90% identical over 60, preferably over 100 nucleotides, more preferably at least 90% identical over 200 nucleotides, or (ii) a nucleic acid sequence complementary to the nucleic acid sequence of SEQ ID NO:1.

Description

field of invention [0001] The present invention relates to protein hydrolysates, methods for producing hydrolysates and uses of these hydrolysates. Background of the invention [0002] Enzymatic hydrolysates of milk or milk components have only limited applications in the food industry. However, these hydrolysates occupy an interesting place in the market, as evidenced by the large number of documents describing and claiming optimized methods for obtaining such hydrolysates. Treatment of milk or milk fractions with enzymes having proteolytic activity to produce hydrolysates, primarily to minimize the allergenicity of the product, facilitate gastrointestinal uptake by providing an easily assimilable digestion, and in acidic Proteins are stabilized in the product to prevent their precipitation during prolonged storage. [0003] While reducing the molecular weight of milk proteins is a generally acceptable procedure to produce these beneficial effects, e...

Claims

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Application Information

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IPC IPC(8): C12N9/50C12N15/57C12N9/62C12N15/63C12N1/19A23K1/165A23JA23KA23K20/147C12NC12R
Inventor P·J·T·戴克R·A·M·范德霍文L·伊登斯L·德兰格
Owner DSM IP ASSETS BV
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