Identification of a novel umami peptide in tempeh (Indonesian fermented soybean) and its binding mechanism to the umami receptor T1R

Muhamad Nur Ghoyatul Amin; Joni Kusnadi; Jue-Liang Hsu; Robert J Doerksen; Tzou-Chi Huang

doi:10.1016/j.foodchem.2020.127411

Identification of a novel umami peptide in tempeh (Indonesian fermented soybean) and its binding mechanism to the umami receptor T1R

Food Chem. 2020 Dec 15:333:127411. doi: 10.1016/j.foodchem.2020.127411. Epub 2020 Jul 4.

Authors

Muhamad Nur Ghoyatul Amin¹, Joni Kusnadi², Jue-Liang Hsu³, Robert J Doerksen⁴, Tzou-Chi Huang⁵

Affiliations

¹ Department of Biological Science and Technology, National Pingtung University of Science and Technology, 1 Shuefu Road, Neipu, Pingtung 91201, Taiwan; Department of Agricultural Product Technology, Faculty of Agricultural Technology, Brawijaya University, Veteran Street, Malang 65145, East Java, Indonesia.
² Department of Agricultural Product Technology, Faculty of Agricultural Technology, Brawijaya University, Veteran Street, Malang 65145, East Java, Indonesia.
³ Department of Biological Science and Technology, National Pingtung University of Science and Technology, 1 Shuefu Road, Neipu, Pingtung 91201, Taiwan. Electronic address: jlhsu@mail.npust.edu.tw.
⁴ Department of BioMolecular Sciences and Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, 209 Graduate House, University, MS, 38677, USA. Electronic address: rjd@olemiss.edu.
⁵ Department of Biological Science and Technology, National Pingtung University of Science and Technology, 1 Shuefu Road, Neipu, Pingtung 91201, Taiwan. Electronic address: tchuang@mail.npust.edu.tw.

PMID: 32682228
DOI: 10.1016/j.foodchem.2020.127411

Abstract

Tempeh, a traditional Indonesian soybean product produced by fermentation, is especially popular because of its umami taste. In this study, a novel umami peptide GENEEEDSGAIVTVK (GK-15) was identified in the small peptide (<3 kDa) fraction of the water extract of tempeh using LC-MS/MS analysis and database-assisted identification. The umami taste of GK-15 was further validated using sensory evaluation, which suggested that GK-15 may be one of the key components contributing to the umami taste in tempeh. To rationalize the biological effect of GK-15, molecular docking of GK-15 into the N-terminal extracellular ligand-binding domain of the umami (T1R) receptor was performed. ZDOCK data showed that GK-15 could perfectly bind either to the open or closed conformation of T1R3. To the best of our knowledge, the present work is the first study to focus on the screening of umami peptides from tempeh.

Keywords: Docking; LC-MS/MS; Peptide; T1R family; Tempeh; Umami.

MeSH terms

Glycine max / metabolism*
Peptides / metabolism*
Protein Binding
Receptors, G-Protein-Coupled / metabolism*
Soy Foods / analysis*
Taste*

Substances

Peptides
Receptors, G-Protein-Coupled
taste receptors, type 1