Thermal degradation of gelatin enhances its ability to bind aroma compounds: Investigation of underlying mechanisms

Qi, Jun; Zhang, Wenwen; Feng, Xianchao; Yu, Jiahang; Han, Minyi; Deng, Shaopo; Zhou, Guanghong; Wang, Huhu

doi:10.1016/j.foodhyd.2018.03.021

Cited by 67 publications

(37 citation statements)

References 52 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%

“…Surface hydrophobicity reflects the number of hydrophobic groups on the protein surface, which can be a suitable parameter for estimating changes in protein exposure and aggregation. 21 As shown in Fig. 2, the surface hydrophobicity of the heat-treated MP solution increased significantly (P < 0.05) as compared with the control, which indicated that more hydrophobic amino acid residues of MP solutions were exposed to the protein surface after thermal treatments.…”

Section: Surface Hydrophobicitymentioning

confidence: 77%

Section: Resultsmentioning

confidence: 99%

“…7), which was similar to the retention of aldehydes by myofibril protein or extracted plant proteins. 13,21 The adsorption capacity of aldehydes in controling MP increased with an increase in chain length. This is supported by an earlier observation by Tan and Siebert, 36 who suggested that the capacity of proteins to bind to aldehydes increased by increasing chain length wileyonlinelibrary.com/jsfa and hydrophobic bonding.…”

Section: Ability Of Aldehydes To Bind To Mpmentioning

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: Surface Hydrophobicitymentioning

confidence: 77%

Section: Resultsmentioning

confidence: 99%

Section: Ability Of Aldehydes To Bind To Mpmentioning

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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“…An increase in the surface hydrophobicity of proteins after heating could improve the corresponding binding ability owing to the exposure of buried hydrophobic amino acid residues on the surface of proteins . Numerous studies have suggested that the increase in hydrophobic bonding sites is responsible for the increasing adsorption affinity of aldehydes . Wang and Arntfield demonstrated that heat treatment created more hydrophobic regions and binding sites, thereby enhancing the flavor‐binding affinity of proteins.…”

Section: Resultsmentioning

confidence: 99%

Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Wang

Zhao

et al. 2019

J Sci Food Agric

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BACKGROUND: The present study investigated the effect of two-step heat treatments on the structure of grass carp myofibrillar proteins (MPs) and their binding ability for selected aldehydes (hexanal, heptanal, octanal and nonanal). RESULTS: Within 30 min of the first heating step at 40 ∘ C and 5-10 min of the second heating step at 90 ∘ C, the enhancement of the flavor-binding ability was likely explained by the increases in surface hydrophobicity and total sulfhydryl content due to the unfolding of secondary structures of MPs through exposure of hydrophobic amino acids and sulfhydryl groups. Nevertheless, lengthy heating at 90 ∘ C accelerated the aggregation of unfolded MPs and reduced the hydrophobic bonding sites, thus weakening the hydrophobic interactions and decreasing the resultant binding ability of MPs with aldehydes.CONCLUSION: The binding ability of aldehydes to MPs was found to be strongly influenced by changes in protein structure and surface during the two-step heating process. The results provided insight into improving the flavor characteristics of freshwater fish surimi products.

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Introduction to Emerging Natural Hydrocolloids

Razavi

2019

Emerging Natural Hydrocolloids

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Thermal degradation of gelatin enhances its ability to bind aroma compounds: Investigation of underlying mechanisms

Cited by 67 publications

References 52 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 aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Introduction to Emerging Natural Hydrocolloids

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