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

被引：68

作者：

Amin, Muhamad Nur Ghoyatul ^{[1
,2
,5
]}

Kusnadi, Joni ^{[2
]}

Hsu, Jue-Liang ^{[1
]}

Doerksen, Robert J. ^{[3
,4
]}

Huang, Tzou-Chi ^{[1
]}

机构：

[1] Natl Pingtung Univ Sci & Technol, Dept Biol Sci & Technol, 1 Shuefu Rd, Pingtung 91201, Taiwan

[2] Brawijaya Univ, Fac Agr Technol, Dept Agr Prod Technol, Veteran St, Malang 65145, East Java, Indonesia

[3] Univ Mississippi, Sch Pharm, Dept BioMol Sci, 209 Grad House, University, MS 38677 USA

[4] Univ Mississippi, Sch Pharm, Res Inst Pharmaceut Sci, 209 Grad House, University, MS 38677 USA

[5] Campus C Univ Airlangga, Fac Fisheries & Marine, Dept Marine, Surabaya 60115, East Java, Indonesia

来源：

FOOD CHEMISTRY | 2020年 / 333卷

关键词：

Tempeh; Umami; Peptide; T1R family; LC-MS/MS; Docking; ENZYME-INHIBITORY PEPTIDES; TASTE; HYDROLYSATE; FRACTIONS; GLUTAMATE; DOCKING;

D O I：

10.1016/j.foodchem.2020.127411

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

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.

引用

页数：9

共 39 条

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