onr:"swepub:oai:DiVA.org:uu-509070"
Search: onr:"swepub:oai:DiVA.org:uu-509070" > Three novel umami p...
- 1 of 1
- Previous record
- Next record
- To hitlist
Three novel umami peptides derived from the alcohol extract of the Pacific oyster (Crassostrea gigas) : identification, characterizations and interactions with T1R1/T1R3 taste receptors
-
- Fu, Baifeng (author)
- Dalian Polytech Univ, Sch Food Sci & Technol, Dalian 116034, Peoples R China.;Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China.
-
- Wu, Di (author)
- Dalian Polytech Univ, Sch Food Sci & Technol, Dalian 116034, Peoples R China.;Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Dalian 116034, Peoples R China.
-
- Cheng, Shuzhen (author)
- Dalian Polytech Univ, Sch Food Sci & Technol, Dalian 116034, Peoples R China.;Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China.;Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Dalian 116034, Peoples R China.
- show more...
- show less...
- Dalian Polytech Univ, Sch Food Sci & Technol, Dalian 116034, Peoples R China;Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China. Dalian Polytech Univ, Sch Food Sci & Technol, Dalian 116034, Peoples R China.;Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Dalian 116034, Peoples R China. (creator_code:org_t)
- Tsinghua University Press, 2024
- 2024
- English.
- In: FOOD SCIENCE AND HUMAN WELLNESS. - : Tsinghua University Press. - 2213-4530. ; 13:1, s. 146-153
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- Oyster (Crassostrea gigas), the main ingredient of oyster sauce, has a strong umami taste. In this study, three potential umami peptides, FLNQDEEAR (FR-9), FNKEE (FE-5), and EEFLK (EK-5), were identified and screened from the alcoholic extracts of the oyster using nano-HPLC-MS/MS analysis, iUmami-Scoring Card Method (iUmami-SCM) database and molecular docking (MD). Sensory evaluation and electronic tongue analysis were further used to confirm their tastes. The threshold of the three peptides ranged from 0.38 to 0.55 mg/mL. MD with umami receptors T1R1/T1R3 indicated that the electrostatic interaction and hydrogen bond interaction were the main forces involved. Besides, the Phe592 and Gln853 of T1R3 were the primary docking site for MD and played an important role in umami intensity. Peptides with two Glu residues at the terminus had stronger umami, especially at the C-terminus. These results contribute to the understanding of umami peptides in oysters and the interaction mechanism between umami peptides and umami receptors. & COPY; 2024 Beijing Academy of Food Sciences. Publishing services by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Subject headings
- NATURVETENSKAP -- Kemi -- Organisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Organic Chemistry (hsv//eng)
Keyword
- Oyster
- umami peptides
- iUmami-SCM
- Taste characterization
- Molecular docking
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
- FOOD SCIENCE AND HUMAN WELLNESS (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Fu, Baifeng
- Wu, Di
- Cheng, Shuzhen
- Xu, Xianbing
- Zhang, Ling
- Wang, Lishu
- show more...
- ElSeedi, Heshanm ...
- Liu, Hanxiong
- Du, Ming
- show less...
- About the subject
-
- NATURAL SCIENCES
- NATURAL SCIENCES
- and Chemical Science ...
- and Organic Chemistr ...
- Articles in the publication
- FOOD SCIENCE AND ...
- By the university
- Uppsala University
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
