Influence of hemin on structure and emulsifying properties of soybean protein isolate

Jiaming Zhang; Yangyang Jia; Wenjin Wu; Yingying Zhang; Ping Chen; Xiaofang Li; Xuetuan Wei; Chunmei Li; Kaikai Li

doi:10.1016/j.foodchem.2023.136183

Influence of hemin on structure and emulsifying properties of soybean protein isolate

Food Chem. 2023 Sep 30:421:136183. doi: 10.1016/j.foodchem.2023.136183. Epub 2023 Apr 23.

Authors

Jiaming Zhang¹, Yangyang Jia², Wenjin Wu³, Yingying Zhang², Ping Chen², Xiaofang Li², Xuetuan Wei², Chunmei Li², Kaikai Li⁴

Affiliations

¹ College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; Shenzhen Institute of Nutrition and Health, Huazhong Agricultural University, Wuhan 430070, China.
² College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
³ Institute for Farm Products Processing and Nuclear-Agricultural Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China.
⁴ College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; Shenzhen Institute of Nutrition and Health, Huazhong Agricultural University, Wuhan 430070, China; Shenzhen Branch, Guangdong Laboratory for Lingnan Modern Agriculture, Genome Analysis Laboratory of the Ministry of Agriculture, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, Shenzhen, China. Electronic address: likaikai@mail.hzau.edu.cn.

PMID: 37116442
DOI: 10.1016/j.foodchem.2023.136183

Abstract

Hemin has potential application value in plant-based meat analogues. However, mechanisms of interaction between hemin and plant protein are unclear. In this study, soy protein isolate (SPI) was applied to examine these interactions using multi-spectroscopic and molecular docking techniques. Additionally, the influence of hemin on emulsification of SPI was also explored. Fluorescence and UV-Vis spectra showed quenching of SPI by hemin was static, resulting in conformation changes on the surface amino acid residues, around which hydrophobicity was significantly reduced from 425.9 ± 16.2 to 108.9 ± 1.8 (p < 0.05). FTIR and CD spectra results suggested the protein secondary structure altered, and the content of α-helix and random coils increased by 1.13% and 1.43%, respectively. Furthermore, emulsifying properties of SPI were strengthened with increased hemin. This work improves our understanding of interactions between SPI and hemin and offer a theoretical basis for application of heme in plant-based meat analogues.

Keywords: Emulsifying ability; Hemin; Interaction mechanism; Soybean protein isolate (SPI).

MeSH terms

Emulsions / chemistry
Hemin*
Hydrophobic and Hydrophilic Interactions
Molecular Docking Simulation
Protein Structure, Secondary
Soybean Proteins* / chemistry

Substances

Soybean Proteins
Emulsions
Hemin