The effects of high pressure treatment on the structural and digestive properties of myoglobin

Qian Li; Hui Liu; Shuai Jiang; Miao Zhang; Kai Shan; Weixin Ke; Di Zhao; Yingqun Nian; Chunbao Li

doi:10.1016/j.foodres.2022.111193

The effects of high pressure treatment on the structural and digestive properties of myoglobin

Food Res Int. 2022 Jun:156:111193. doi: 10.1016/j.foodres.2022.111193. Epub 2022 Mar 26.

Authors

Qian Li¹, Hui Liu¹, Shuai Jiang¹, Miao Zhang¹, Kai Shan¹, Weixin Ke¹, Di Zhao¹, Yingqun Nian¹, Chunbao Li²

Affiliations

¹ Key Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
² Key Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: chunbao.li@njau.edu.cn.

PMID: 35651048
DOI: 10.1016/j.foodres.2022.111193

Abstract

The effects of high pressure treatment (100-400 MPa for 20 min) on the structural and digestive properties of myoglobin were investigated by UV-vis absorption spectroscopy, intrinsic and synchronous fluorescence spectroscopy and molecular dynamics simulation. High pressure treatment induced the exposure of aromatic residues and changed the interaction between heme and globin, which in turn increased the gastrointestinal digestibility of myoglobin. Molecular dynamics simulation indicated that the hydrophobic interaction and hydrogen bonds of the myoglobin-pepsin complex were weakened after high pressure treatment, but the dipolar interaction was strengthened. The findings revealed the mechanisms on high pressure-induced increase in digestibility of myoglobin.

Keywords: Binding mode; Digestibility; High pressure treatment; Myoglobin; Structural changes.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Heme*
Hydrogen Bonding
Myoglobin*
Pepsin A / chemistry
Spectrometry, Fluorescence

Substances

Myoglobin
Heme
Pepsin A