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Cited by 72Biochemical Analysis and Sensing TechniquesProtein Hydrolysis and Bioactive PeptidesFood Nutrient Composition and Product Development

The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.

The behavior of umami components in thermally treated yeast extract

Abstract

Umami proteolytics are natural food flavor alternatives to glutamate. In this study, key umami taste fractions were separated and purified from thermally treated yeast extract (YE) to yield fifteen umami peptides. Systematic approaches using sensory-guided fractionation on taste-active umami proteolytics separation and detection were utilized. A reaction temperature of 110 °C was optimum for umami peptide generation. Under this reaction temperature, the sensory score and E-tongue results of umami taste were the highest. The sensory evaluation-based taste dilution analysis and taste threshold determination supported the hypothesis that umami peptides have their physiological effect by binding to G-protein coupled receptors. The structural differences of umami peptides contribute to their taste profile and allow categorization into two group Types. Fifteen umami peptides were then categorized into Type I and Type II regarding the contractual-based taste mechanism: Type I peptides imparted complex tastes. The tastes of Type I peptides could split into two stages: bitterness and umami in pure water, whereas, Type II peptides presented strong umami taste at a high concentration in pure water, and the relationship between umami capacity and peptides concentration was linear. Finally, the guidance of the umami peptide usage in the flavor industry has been established according to broths dissolution test.

Overview

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Registry

Crossref · 10.1016/j.foodres.2018.11.002

Cites

52 of 52 references verified0 citation errors · 0 not checkable

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Citations

Cites

Show all 51 references

Research works printed but not linked: 2

  1. Ishibashi, 1988, Studies on flavored peptides. Part III. Role of the hydrophobic amino acid residue in the bitterness of peptides, Agricultural & Biological Chemistry, 52, 91
  2. Matsushita, 1965, Purification and sequence determination of tasty tetrapeptide (Asp-Asp-Asp-Asp) from beer yeast seasoning and its enzymatic synthesis, Peptide Chemistry, 323, 249

Cited by

See all 72

Metadata

Authors
Alim, A., Yang, C., Song, H., Liu, Y., Zou, T., Zhang, Y., & Zhang, S.
Affiliations
Beijing Technology and Business University (CN)
Corresponding author
Song, Huanlu
Venue
Food Research International
Publisher
Elsevier BV
Published
2019-06
Volume
120
Pages
534-543
ISSN
0963-9969 (ISSN-L)
OpenAlex
W2900173274
Cited by
71
References
51
Citations by year
2026: 8 · 2025: 13 · 2024: 16 · 2023: 7 · 2022: 12 · 2021: 5 · 2020: 8 · 2019: 2
FWCI
2.99
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Food Research International (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Natural Science Foundation of China (31571884)
Topics
  • Health Sciences › Nursing › Nutrition and Dietetics › Biochemical Analysis and Sensing Techniques
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Food Nutrient Composition and Product Development
Keywords
umami peptides, yeast extract, heat treatment (food and biological processing), umami taste, G protein-coupled receptors, taste threshold, broth
MeSH terms
Biological Products, Flavoring Agents, Peptides, Yeasts, Electronic Nose

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Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.