Binding of safranal to whey proteins in aqueous solution: Combination of headspace solid-phase microextraction/gas chromatography with multi spectroscopic techniques and docking studies.


Journal

Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639

Informations de publication

Date de publication:
30 Jul 2019
Historique:
received: 10 11 2018
revised: 12 02 2019
accepted: 14 02 2019
entrez: 13 3 2019
pubmed: 13 3 2019
medline: 30 5 2019
Statut: ppublish

Résumé

The objective of this work was to study molecular binding of safranal to whey proteins by taking advantage of headspace solid-phase microextraction combined with gas chromatography (HS-SPME/GC), fluorescence and circular dichroism (CD) spectroscopies, and docking studies. The results of HS-SPME/GC indicated that bovine serum albumin (BSA) had the highest affinity toward safranal, with binding constant of 3.196 × 10

Identifiants

pubmed: 30857705
pii: S0308-8146(19)30388-7
doi: 10.1016/j.foodchem.2019.02.065
pii:
doi:

Substances chimiques

Cyclohexenes 0
Lactoglobulins 0
Terpenes 0
Whey Proteins 0
Serum Albumin, Bovine 27432CM55Q
safranal 4393FR07EA
Lactalbumin 9013-90-5

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

313-323

Informations de copyright

Copyright © 2019 Elsevier Ltd. All rights reserved.

Auteurs

Samira Feyzi (S)

Department of Food Science and Technology, Faculty of Agriculture, Ferdowsi University of Mashhad, Mashhad, Iran. Electronic address: sa.feyzi@mail.um.ac.ir.

Mehdi Varidi (M)

Department of Food Science and Technology, Faculty of Agriculture, Ferdowsi University of Mashhad, Mashhad, Iran. Electronic address: m.varidi@um.ac.ir.

Mohammad Reza Housaindokht (MR)

Department of Chemistry, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran. Electronic address: housain@um.ac.ir.

Zarrin Es'haghi (Z)

Department of Chemistry, Payame Noor University, 19395-4697 Tehran, Iran. Electronic address: eshaghi@pnu.ac.ir.

Articles similaires

Animals Hemiptera Insect Proteins Phylogeny Insecticides
Adenosine Triphosphate Adenosine Diphosphate Mitochondrial ADP, ATP Translocases Binding Sites Mitochondria

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones
Fucosyltransferases Drug Repositioning Molecular Docking Simulation Molecular Dynamics Simulation Humans

Classifications MeSH