Conformational changes induced by selected flavor compounds from spices regulate the binding ability of myofibrillar proteins to aldehyde compounds.
Autor: | Sun X; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; Integrated Laboratory of Processing Technology for Chinese Meat and Dish Products, Ministry of Agriculture and Rural Affairs, Beijing 100193, China; College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China., Yu Y; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; Integrated Laboratory of Processing Technology for Chinese Meat and Dish Products, Ministry of Agriculture and Rural Affairs, Beijing 100193, China., Saleh ASM; Department of Food Science and Technology, Faculty of Agriculture, Assiut University, Assiut 71526, Egypt., Akhtar KH; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; Integrated Laboratory of Processing Technology for Chinese Meat and Dish Products, Ministry of Agriculture and Rural Affairs, Beijing 100193, China., Li W; College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China., Zhang D; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; Integrated Laboratory of Processing Technology for Chinese Meat and Dish Products, Ministry of Agriculture and Rural Affairs, Beijing 100193, China., Wang Z; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; Integrated Laboratory of Processing Technology for Chinese Meat and Dish Products, Ministry of Agriculture and Rural Affairs, Beijing 100193, China. Electronic address: caasjgsmeat2021_1@126.com. |
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Jazyk: | angličtina |
Zdroj: | Food chemistry [Food Chem] 2024 Sep 01; Vol. 451, pp. 139455. Date of Electronic Publication: 2024 Apr 24. |
DOI: | 10.1016/j.foodchem.2024.139455 |
Abstrakt: | Interactions among flavor compounds from spices (FCS) and myofibrillar proteins (MP) were investigated. Fluorescence and Fourier transform infrared spectroscopy showed that hydrogen bonding and hydrophobic interactions were the main binding forces between FCS and MP. The FCS increased the particle size and SH content of MP and caused a reduction of zeta potential from -5.23 to -6.50 mV. Furthermore, FCS could modify the binding ability of MP and aldehydes. Eugenol reduced the ability of MP to bond with aldehydes by 22.70-47.87 %. Molecular dynamics simulations demonstrated that eugenol may combat nonanal to attain binding site of amino acid residue (PHE165) and induce protein conformational changes. Electrostatic interactions and van der Waals forces within myosin-nonanal may be disrupted by these alterations, which could reduce stability of complex and cause release of nonanal. This study could provide new insights into regulating the ability of proteins to release and hold flavors. Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (Copyright © 2024 Elsevier Ltd. All rights reserved.) |
Databáze: | MEDLINE |
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