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Bitterness of Peptides: Amino Acid Composition and Chain Length
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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“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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Debittering of protein hydrolyzates
Badal Chandra, S. A. H. A., & Hayashi, K. (2001) · Biotechnology Advances · doi:10.1016/s0734-9750(01)00070-2 · Cited by 229
Peptides From Milk Proteins and Their Properties
Kilara, A., & Panyam, D. (2003) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408690390251138 · Cited by 230
“Ney (1979) reported that hydrolyzates from common food proteins containing a preponderance of peptides below an apparent molecular weight of 6000 would certainly be bitter.”
BackgroundThe potential role of secondary metabolites in modulating the flavor and taste of the meat
Ramalingam, V., Song, Z., & Hwang, I. (2019) · Food Research International · doi:10.1016/j.foodres.2019.04.007 · Cited by 220
Lemieux, L., & Simard, R. E. (1992) · Le Lait · doi:10.1051/lait:1992426 · Cited by 210
“Bitter taste of peptides in relation to theïr average hydrophobicity Q and molecular weight (Ney, 1979).”
BackgroundInfluentialLiu, B., Li, N., Chen, F., Zhang, J., Sun, X., Xu, L., & Fang, F. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13050 · Cited by 206
Metadata
- 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
- 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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