Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractObstacle avoidance planning of space manipulator end-effector based on improved ant colony algorithm    Next AbstractGenome-wide transcriptional changes and defence-related chemical profiling of rice in response to infestation by the rice striped stem borer Chilo suppressalis »

J Agric Food Chem


Title:Binding of aroma compounds with myofibrillar proteins modified by a hydroxyl-radical-induced oxidative system
Author(s):Zhou F; Zhao M; Su G; Sun W;
Address:"College of Light Industry and Food Science, South China University of Technology , Guangzhou 510640, China"
Journal Title:J Agric Food Chem
Year:2014
Volume:20140916
Issue:39
Page Number:9544 - 9552
DOI: 10.1021/jf502540p
ISSN/ISBN:1520-5118 (Electronic) 0021-8561 (Linking)
Abstract:"The objective of this study was to investigate the influence of oxidation-induced structural modifications of myofibrillar protein on its binding ability with aroma compounds such as 2-methyl-butanal, methional, 2-pentanone, 2-heptanone, and nonanal. A method using solid-phase microextraction (SPME) combined with gas chromatography/mass spectrometry (GC/MS) was used to determine the corresponding binding ability. The binding with aroma compounds was found to be strongly affected by the oxidation levels of proteins, probably due to the varying modifications in protein structure and surface. Incubation with oxidants around or below 1 mM mainly caused the refolding of protein structure and accelerated the protein aggregation, which reduced the affinity of the aroma compounds, thus decreasing the binding ability. Nevertheless, treatment with oxidants over 2.5 mM would cause protein reaggregation and partial degradation, and thus, the subsequent modification of protein surface properties. The aggregated protein with wrinkled surfaces favored the hydrophobic interactions with aroma compounds, forming the protein-aroma compound complex, thus enhancing the resultant binding ability as evidenced by fluorescence quenching and SPME-GC/MS analysis"
Keywords:Animals Gas Chromatography-Mass Spectrometry Hydroxyl Radical/*chemistry Meat/*analysis Muscle Proteins/*chemistry Myofibrils/*chemistry Oxidation-Reduction Protein Binding Smell Solid Phase Microextraction Swine Volatile Organic Compounds/*chemistry Spme;
Notes:"MedlineZhou, Feibai Zhao, Mouming Su, Guowan Sun, Weizheng eng Research Support, Non-U.S. Gov't 2014/09/02 J Agric Food Chem. 2014 Oct 1; 62(39):9544-52. doi: 10.1021/jf502540p. Epub 2014 Sep 16"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 26-12-2024