Binding of selected volatile flavour mixture to salt-extracted canola and pea proteins and effect of heat treatment on flavour binding

Wang, Kun; Arntfield, Susan D.

doi:10.1016/j.foodhyd.2014.06.011

Cited by 90 publications

(74 citation statements)

References 37 publications

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“…The binding ability of selected aldehydes among all samples was 21 to 27% (Fig. ), which was similar to the retention of aldehydes by myofibril protein or extracted plant proteins . The adsorption capacity of aldehydes in controling MP increased with an increase in chain length.…”

Section: Resultssupporting

confidence: 64%

“…The flavor compounds were then added to 5 mg mL −1 of preheated or unheated MP solutions and shaken for 30 s, resulting in a final concentration of 1 ppm for each compound. The binding capacity of MP was determined according to the method of Wang and Arntfield with slight modification. Ten milliliters of the mixture were carefully loaded into a 20 mL headspace vial and immediately sealed with PTFE/silicone septa and magnetic metal crimp caps.…”

Section: Methodsmentioning

confidence: 99%

“…The quantity of flavor compounds was determined according to the method of Wang and Arntfield with slight modification. The capacity of flavor compounds to bind to protein was measured using an Agilent 7890 gas chromatography‐5975C quadropole mass selective detector (Agilent Technologies, Santa Clara, California, USA), equipped with an HP‐5MS capillary column (30 m length × 0.25 mm I.D.…”

Section: Methodsmentioning

confidence: 99%

“…Heat treatment is an essential step in the processing of surimi products, leading to the dissociation and unfolding of proteins, with subsequent aggregation and production of conformational changes in the secondary and tertiary structure of the protein . However, the effects of heat treatment on the flavor binding affinity of proteins have been reported with conflicting results, indicating both increases and decreases . Kühn et al .…”

Section: Introductionmentioning

confidence: 99%

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Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Zhao

Wang

et al. 2019

J Sci Food Agric

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BACKGROUND The influence of heat‐induced structural modifications of grass carp myofibrillar protein (MP) on its ability to bind to selected aldehydes (hexanal, heptanal, octanal and nonanal) was investigated. The interactions of MP and flavor compounds were investigated using HS‐GC‐MS, intrinsic fluorescence spectra, Raman spectra, SDS‐PAGE, turbidity, total sulfhydryl content and surface hydrophobicity. RESULTS The ability to bind to aldehydes was strongly influenced by changes in the structure and surface of proteins during the heating process (0–30 min). During the first 0–10 min of heating, the flavor‐binding ability increased, which is likely attributable to increased surface hydrophobicity and total sulfhydryl content, and to the unfolding of secondary structures of MP by exposure to reactive amino acids, sulfhydryl groups and hydrophobic bonding sites. Nevertheless, lengthy heating (>10 min) caused protein refolding and accelerated aggregation of protein, thus reducing hydrophobic interactions and weakening the resultant capacity of MP to bind to flavor compounds. CONCLUSION The results suggested that hydrophobic interactions were enhanced upon short‐term heating, whereas long‐term heating weakend them. The results provide information concerning improvement of the flavor profile of freshwater fish surimi products. © 2019 Society of Chemical Industry

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Section: Resultssupporting

confidence: 64%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Zhao

Wang

et al. 2019

J Sci Food Agric

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“…Damodaran and Kinsella (a) suggested that the association among SPI subunits might form high‐affinity primary binding sites of hydrophobic cavities at their interfaces, which act as binding sites for carbonyls at pH 8.0; however, equilibrium dialysis technology is based on higher flavor concentration, which reaches saturation levels of the primary binding sites. At high concentration levels, the binding force that is enough to change the conformation of the protein also induced new binding sites (Kühn, Considine, & Singh, ; Wang & Arntfield, ). The primary binding sites of SPI need more sensitive technology to determinate the free flavoring compounds at an unsaturation level.…”

Section: Resultsmentioning

confidence: 99%

Binding of aromatic compounds with soy protein isolate in an aqueous model: Effect of pH

Guo

et al. 2019

J Food Biochem

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Interactions of the flavoring compounds hexyl acetate (HxAc), heptyl acetate (HpAc), linalyl formate (LiFo), linalyl acetate (LiAc), geraniol, linalool, limonene, and myrcene with soy protein isolate (SPI) were estimated in pH 3.0, 6.0, and 9.0 aqueous solutions using headspace solid‐phase microextraction gas chromatography–mass spectrometry (SPME–GC–MS). The binding capacity of HxAc, HpAc, LiFo, LiAc, geraniol, and linalool increased in the pH of the medium from 3 to 9. For limonene and myrcene, an unexpected increase in headspace concentration or a “salting‐out” effect was observed. Between pH 3 and 9, better accessibility to the primary hydrophobic sites as a result of a modification to the protein's flexibility was observed. Practical applications SPME method is a technology of dynamic adsorption for flavors. The lowest level of lead be practicably detected in food as low as the practiced concentration of flavors (0.01–0.1 mM) in our study. At low concentrations of flavors, it is close to the actual flavor's concentration of food. In the previous studies, the technology, such as equilibrium dialysis, headspace‐gas phase which need higher concentration of flavors (>0.2 mM). The interaction between flavors and protein has a different binding law at high and low concentrations. As we produced the acid fruit soy protein milk beverage, the off‐flavors present in the beverage were due to the change in the interaction between denature SPI and flavors. The present work is aimed at paving the way for further research to elucidate flavor imbalances in acid fruit soy protein milk beverage.

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Artificial Nanostructures in Food

Raynes

Gras

Carver

et al. 2017

Nanotechnology in Agriculture and Food Science

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Binding of selected volatile flavour mixture to salt-extracted canola and pea proteins and effect of heat treatment on flavour binding

Cited by 90 publications

References 37 publications

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Binding of aromatic compounds with soy protein isolate in an aqueous model: Effect of pH

Artificial Nanostructures in Food

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