Cited by 152Biochemical Analysis and Sensing TechniquesProtein Structure and DynamicsChemical Synthesis and Analysis

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Bitterness of Peptides: Amino Acid Composition and Chain Length

NEY, KARL HEINZ·1979·ACS Symposium Series

DOI 10.1021/bk-1979-0115.ch006

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Abstract

During our work on taste of foods we synthesized a series of peptides and soon came to the opinion, that the bitterness of peptides is caused by the hydrophobic action of amino acid side chains. Here I think some remarks on hydrophobic interactions ( 1 ) would be appropriate. It is generally accepted now, that hydrophobic interactions are a contributing factor to protein behaviour and esp. to the formation of the secondary structure, e.g. helix. This means, that as shown in Figure 1 hydrophobic residues of the amino acids in a peptide are driven together by clusters of water molecules and so the secondary structure of a peptide or protein is formed. For the transfer from the helical to the stretched form, Tanford ( 2 ) found that the transfer free energy of the total protein results from the sum of the contributions of the single amino acid residues. The Δf values of the

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“However, this principle is valid for peptides with molecular weights up to approximately 6000 Daltons; above this limit peptides with a Q-value above 1400 are also not bitter (Ney, 1979).”
Background
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“Ney [67] confirmed that the degree of hydrophobicity of peptides is the most important indicator of their bitterness and established the Q-rule to evaluate this trait.”
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Murray, N. M., O’Riordan, D., Jacquier, J., et al. (2017) · Journal of Sensory Studies · doi:10.1111/joss.12266 · Cited by 7
“Studies have investigated the bitterness of synthesized peptides and reported links between low molecular weight, hydrophobic peptides, and increased bitterness (Ney, 1979), as well as the positioning of amino acids within the peptide chain (Ishibashi, Arita, et al.”
Influential
Enzymic hydrolysis of fish offal without added water
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“The hydrophobic index, determined as the Q-value, was calculated for the identified peptides to predict their bitterness potential using the algorithm proposed by Ney [29].”
Method
Tilsiter‐Aroma
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Self-citation
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“As was expected by Ney’s Q-value (Ney, 1973, 1978), average hydrophobicity of the wheat gluten hydrolysate was under 1400 cal/mol.”
Method
Selective Removal of Hydrpphobic Peptides from Protein Hydrolysates in a Continuous Supported Liquid Membrane Process
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“The requirement demanded in the formation of hydrolysates is that they should not have a bitter taste, should be hypoallergenic, should be low in free amino acids (Ney, 1979; Grimble et al., 1986; Otani et al., 1990).”
Background
Production of casein hydrolysates by extracellular acid proteinases of immobilized Humicola lutea cells
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“According to Ney (1972) proteins with Q values > 1400 cal/mol have a bitter taste (casein Q value = 1605 cal/mol), which does not appear if the molecular mass of the peptide fragments exceeds 6 kDa (Ney 1979).”
Background
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Lee, C. K., Koh, L. L., & Xu, Y. (1995) · Food Chemistry · doi:10.1016/0308-8146(94)p4196-m
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“In pH-stat hydrolysis the reaction pH is maintained at the enzyme's optimum by continuous alkali titration, whereas in free-fall pH mode the pH decreases naturally as hydrolysis proceeds (Ney and Boudreau, 1979).”
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Authors: NEY, K. H.
Affiliations: Unilever (Germany) (DE)
Corresponding author: NEY, KARL HEINZ
Venue: ACS Symposium Series
Publisher: AMERICAN CHEMICAL SOCIETY
Published: 1979-12-14
Pages: 149-173
ISSN: 0097-6156 (ISSN-L)
1947-5918
DOI: 10.1021/bk-1979-0115.ch006
OpenAlex: W2506737813
Cited by: 152
References: 0
Citations by year: 2026: 5 · 2025: 8 · 2024: 5 · 2023: 5 · 2022: 10 · 2021: 5 · 2020: 4 · 2019: 9 · 2018: 9 · 2017: 6 · 2016: 4 · 2015: 2 · 2014: 6 · 2013: 6
FWCI: 4.00
Type: conference paper
Language: en
Open access: closed
Locations: ACS symposium series (publishedVersion)
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Biochemical Analysis and Sensing Techniques
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Keywords: amino acid composition, chain length, hydrophobic interactions, amino acid side chains, peptide secondary structure, helix formation, water clusters, transfer free energy

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Bitterness of Peptides: Amino Acid Composition and Chain Length

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