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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Background
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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…”
Method
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Method
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Method
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“The bitterness elicited by peptides has been researched by numerous authors who found that bitterness is most commonly associated with; small to medium hydrophobic peptides (Ney, 1979), peptides with high proline content (Ishibashi, Kubo, et al.”
Background
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“According to Ney (1979) bitterness of peptides is associated with the degree of hydrophobici ty of amino acid side chains and the length of the peptide produced.”
Background
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BackgroundInfluential
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Background
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Bouroutzika, E. V., Proikakis, S., Anagnostopoulos, A. K., Katsafadou, A. I., Fthenakis, G. C., & Tsangaris, G. T. (2021) · Applied Sciences · doi:10.3390/app11167622 · Cited by 23
“Graviera Kritis RP-HPLC analysis SDS PAGE [28]”
BackgroundInfluential
Characterization of bitter peptides in casein hydrolysates using comprehensive two-dimensional liquid chromatography
Höhme, L., Fischer, C., & Kleinschmidt, T. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.134527 · Cited by 21
Functional Properties of Fish Protein Hydrolysates
Pires, C., & Batista, I. (2013) · CRC Press eBooks · doi:10.1201/b14944-4 · Cited by 21
Identifying Sequential Residue Patterns in Bitter and Umami Peptides
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Antimicrobial peptides derived from food byproducts: Sources, production, purification, applications, and challenges
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Analysis of the Seasonal Change of the Proximate Composition and Taste Components in the Conger Eels (Conger myriaster)
Ryu, K.-Y., Shim, S., Kim, W. B., et al. (2009) · Journal of the Korean Society of Food Science and Nutrition · doi:10.3746/jkfn.2009.38.8.1069 · Cited by 20
“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
Lv, J., Geng, A., Pan, Z., et al. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169005 · Cited by 19
Effect of dry heat on the in vitro digestibility and trypsin inhibitor activity of chickpea flour
Márquez, Fernández, & Alonso (1998) · International Journal of Food Science & Technology · doi:10.1046/j.1365-2621.1998.00218.x · Cited by 19
Comparative Analysis of Purine Alkaloids and Main Quality Components of the Three Camellia Species in China
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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
Isolation, identification and sensory evaluation of kokumi peptides from by‐products of enzyme‐modified butter
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Response surface optimization of enzymatic hydrolysis of duck blood corpuscle using commercial proteases
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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
Daher, D., Deracinois, B., Baniel, A., et al. (2020) · Foods · doi:10.3390/foods9101354 · Cited by 16
“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
Aubes-Dufau, I., & Combes, D. (1997) · Applied Biochemistry and Biotechnology · doi:10.1007/bf02787847 · Cited by 15
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
Wang, K.-Z., Xu, W., Zhou, M., et al. (2018) · Aquaculture Nutrition · doi:10.1111/anu.12677 · Cited by 14

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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