Bitterness of peptides: Amino acid composition and chain length

NEY, KARL HEINZ

doi:10.1021/bk-1979-0115.ch006

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

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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A peptide with Q value above 1400 is bitter; below 1300 it is not bitter; bitterness between 1300 and 1400 cannot be predicted.
“When this value exceeds 1400, the peptide is to be considered bitter, while below 1300, the peptide is not bitter, but the bitterness of a peptide that has a Q value between 1300 and 1400 cannot be predicted [82].”
From Plant Milk-Clotting Enzymes for Cheesemaking (2022) · cites this paper as [82]

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“According to Ney’s method (Ney, 1979) the average hydrophobic value was calculated as follows: Q = ∑ DQ = AAi/Mi∑ AAi/Mi × Dfti (1) where AAi is content of each amino acid in 100 g protein (g), Mi is molar mass of each amino acid (g/mol), ∑AAi/Mi was the total moles of amino acid in 100 g of…”
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Background
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Background
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BackgroundInfluential
Quantitative Structure–Activity Relationship Study of Bitter Di-, Tri- and Tetrapeptides Using Integrated Descriptors
Xu, B., & Chung, H. Y. (2019) · Molecules · doi:10.3390/molecules24152846 · Cited by 27 · see citing works
“For example, with a stronger hydrophobicity of C-terminal amino acid “F” [4f value (measurement of hydrophobicity) of 2650] than C-terminal amino acid “V” (4f value of 1690), dipeptide “AF” (19 mM) showed a lower bitter taste threshold than dipeptide “AV” (69 mM) [5,38].”
Background
Structural Characteristics of Food Protein‐Derived Bitter Peptides
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“Graviera Kritis RP-HPLC analysis SDS PAGE [28]”
BackgroundInfluential
Characterization of bitter peptides in casein hydrolysates using comprehensive two-dimensional liquid chromatography
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“Histidine은 백색육 어류보다 적색육 어류에 많이 존재하는 아미노산이나(17), Ney(34)는 미각 테스트 결과 고등어나 참 치에서 많이 함유되어 있는 histidine은 이들 어류의 맛에 중요한 역할을 하고 있지 않은 것으로 보고하여, 붕장어에서 정미성분으로서의 역할은 크기 않을 것으로 생각된다.”
iBitter-GRE: A Novel Stacked Bitter Peptide Predictor with ESM-2 and Multi-View Features
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Effect of dry heat on the in vitro digestibility and trypsin inhibitor activity of chickpea flour
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“Amino acids can exhibit various taste characteristics in tea, including umami, sweet, sour, or even bitter, the latter caused by the hydrophobic effect of amino acid side chains [40].”
Background
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Gamma-glutamylation of beef protein hydrolysates to improve its overall taste and functions of gastro-intestinal hormone (CCK and GLP-1) pro-secretion and anti-inflammation
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“The Q value for evaluating bitterness was calculated on the basis of the free energy values of amino acid side chains and determined to be 1,091 cal/mol (<1,300 cal/mol), indicating no bitter taste in the BCH (Ney, 1979; FitzGerald and O’cuinn, 2006).”
MethodInfluential
Principal Component Analysis from Mass Spectrometry Data Combined to a Sensory Evaluation as a Suitable Method for Assessing Bitterness of Enzymatic Hydrolysates Produced from Micellar Casein Proteins
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“The bitterness of a peptide can also be related to the hydrophobic nature of its amino acids [22], such as aromatic residues (tryptophan, tyrosine, and phenylalanine) or having a hydrocarbon side chain (leucine, isoleucine, and valine) and their position in the peptide sequence [23].”
Background
Effect of different proteases on bitterness of hemoglobin hydrolysates
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Identification and Characterization of the Off-Flavor in Mantle Muscle of Jumbo Squid (Dosidicus gigas) from the Gulf of California
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Effects of fishmeal replacement with cottonseed meal protein hydrolysate on growth, digestion and intestinal histology of juvenile Chinese soft-shelled turtle,Pelodiscus sinensis
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The Configuration of Polypeptide Chains in Proteins
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Amino acid distribution in protein secondary structures
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Helix Propensities of Amino Acid Residues via Thioester Exchange
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Chou-Fasman analysis of the secondary structure of F and Le interferons
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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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 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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