The ability of peptide extracts obtained at different dry cured ham ripening stages to bind aroma compounds

Martínez-Arellano, Isadora; Flores, Mónica; Toldrá, Fidel

doi:10.1016/j.foodchem.2015.09.023

Cited by 34 publications

(24 citation statements)

References 36 publications

(35 reference statements)

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“…As previously reported, the nature of the bonds between aldehydes and proteins is two‐fold: reversible hydrophobic, hydrogen bonds and irreversible covalent bonds with amino and sulfhydryl groups . Changes in protein conformation could affect flavor‐binding ability because of the modification of available binding sites .…”

Section: Resultsmentioning

confidence: 92%

“…An increase in surface hydrophobicity after 1, 2, 5 and 10 min of heating (Fig. ) could enhance the affinity of flavor compounds to proteins through hydrophobic interaction, as the result of exposure of buried hydrophobic regions on the surface of the protein . Moreover, the decreases in content of the α‐helix (Table ) and intrinsic fluorescence intensity (Fig.…”

Section: Resultsmentioning

confidence: 97%

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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: Resultsmentioning

confidence: 92%

Section: Resultsmentioning

confidence: 97%

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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“…As a traditional food with broad consumer acceptance and unique local characteristics, dry‐cured ham represents the cultural heritage of a region. However, most dry‐cured hams in the market are made of pork (Harkouss et al, ; Martínez‐Arellano et al, ; Petrova, Aasen, Rustad, & Eikevik, ; Toldra, ). Mutton, a high‐protein, low‐fat, and low‐cholesterol meat, is expected to gain popularity as an alternative to pork in dry‐cured hams (Zhang, Yoo, Gathercole, Reis, & Farouk, ).…”

Section: Introductionmentioning

confidence: 99%

Correlations among flavor compounds, lipid oxidation indices, and endogenous enzyme activity during the processing of Xinjiang dry‐cured mutton ham

Guo

Lü

Wang

et al. 2019

J Food Process Preserv

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Mutton is widely consumed in China, European Mediterranean countries, and other regions around the world and is expected to gain popularity as an alternative to pork in dry‐cured hams. Changes in the physicochemical indices, volatile compounds, and endogenous enzyme activities during the processing of dry‐cured mutton ham were investigated. Eighty‐six volatile compounds were identified during the dry‐curing process, with aldehydes being dominant. Oxidation values increased significantly during dry‐curing and decreased during ripening (p < .05). The activities of lipolytic enzymes remained active throughout processing, although the activities of the enzymes decreased. Lipoxidase activity increased rapidly during the fermenting stage and then decreased gradually during ripening (p < .05). Superoxide dismutase activity increased throughout processing, whereas the catalase activity decreased. According to partial least square variable importance in projection analysis, 49 odor‐related compounds were selected from dry‐cured mutton ham as specific compounds which are related to lipid oxidation and endogenous enzyme activities. Heatmap shows that the volatile compounds were correlated with enzyme activity and the oxidation value of dry‐cured mutton ham during processing. Practical applications Xinjiang dry‐cured mutton ham has an intense and a long‐lasting aroma. Understanding the mechanism of aroma formation related to lipid oxidation could help us to improve the product quality and optimize the duration of processing. Therefore, the present work identified the characteristic flavor compounds and provided the changing regularity of these compounds at various stages to facilitate the generation of them.

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“…These biochemical reactions give rise to volatile compounds such as aldehydes, alcohols, ketones, carboxylic acids, esters, sulfur compounds, nitrogenous compounds, and aromatic and cyclic hydrocarbons (Wang and others ). These contribute to the development of the typical flavor of dry‐cured hams (Vestergaard and others ; Arnau and others ; Ventanas and others ; Marušić and others ; Narváez‐Rivas and others ; Martínez‐Arellano and others ).…”

Section: Introductionmentioning

confidence: 99%

Contribution of Histidine and Lysine to the Generation of Volatile Compounds in Jinhua Ham Exposed to Ripening Conditions Via Maillard Reaction

Zhu

Zhao

Tian

et al. 2017

Journal of Food Science

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To evaluate the role of Maillard reactions in the generation of flavor compounds in Jinhua ham, the reactions of glucose and ethanal with histidine and lysine, respectively, were studied by simulating the ripening conditions of Jinhua ham. The volatile products produced were analyzed using solid phase microextraction-gas chromatography/mass spectrometry. The results showed that 8 volatile compounds were generated by the reaction of glucose and histidine and 10 volatile compounds were generated by the reaction of glucose and lysine. Reactions of ethanal with lysine and with histidine both generated 31 volatile compounds that contributed to the flavor of Jinhua ham. This indicates that histidine and lysine related to Maillard reactions possibly play important roles in the generation of the unique flavor compounds in Jinhua ham. This research demonstrates that free amino acids participate in the generation of volatile compounds from Jinhua ham via the Maillard reaction and provides a basic mechanism to explain flavor formation in Jinhua ham.

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The ability of peptide extracts obtained at different dry cured ham ripening stages to bind aroma compounds

Cited by 34 publications

References 36 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

Correlations among flavor compounds, lipid oxidation indices, and endogenous enzyme activity during the processing of Xinjiang dry‐cured mutton ham

Contribution of Histidine and Lysine to the Generation of Volatile Compounds in Jinhua Ham Exposed to Ripening Conditions Via Maillard Reaction

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