Conformational changes induced by selected flavor compounds from spices regulate the binding ability of myofibrillar proteins to aldehyde compounds

Xiangxiang Sun; Yumei Yu; Ahmed S M Saleh; Kumayl Hassan Akhtar; Wenhao Li; Dequan Zhang; Zhenyu Wang

doi:10.1016/j.foodchem.2024.139455

Conformational changes induced by selected flavor compounds from spices regulate the binding ability of myofibrillar proteins to aldehyde compounds

Food Chem. 2024 Apr 24:451:139455. doi: 10.1016/j.foodchem.2024.139455. Online ahead of print.

Authors

Xiangxiang Sun¹, Yumei Yu², Ahmed S M Saleh³, Kumayl Hassan Akhtar², Wenhao Li⁴, Dequan Zhang², Zhenyu Wang⁵

Affiliations

¹ 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.
² 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.
³ Department of Food Science and Technology, Faculty of Agriculture, Assiut University, Assiut 71526, Egypt.
⁴ College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China.
⁵ 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.

PMID: 38678659
DOI: 10.1016/j.foodchem.2024.139455

Abstract

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.

Keywords: Adsorption properties; Aldehydes; Flavor compounds; Myofibrillar protein.