Overheating induced structural changes of type I collagen and impaired the protein digestibility

Miao Zhang; Di Zhao; Shuran Zhu; Yingqun Nian; Xinglian Xu; Guanghong Zhou; Chunbao Li

doi:10.1016/j.foodres.2020.109225

Overheating induced structural changes of type I collagen and impaired the protein digestibility

Food Res Int. 2020 Aug:134:109225. doi: 10.1016/j.foodres.2020.109225. Epub 2020 Apr 7.

Authors

Miao Zhang¹, Di Zhao¹, Shuran Zhu¹, Yingqun Nian¹, Xinglian Xu¹, Guanghong Zhou¹, 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: 32517907
DOI: 10.1016/j.foodres.2020.109225

Abstract

Collagen, especially type I collagen, a major component for connective tissue in meat, determines the background tenderness and affects digestibility of meat. Heating may induce great changes in protein structure and its pepsin-treated digestion. The objective of this study was to investigate how heating affected type I collagen structure and in vitro pepsin-treated digestion. Type I collagen was heated at 60 °C, 70 °C, 80 °C for 0.5 to 2.5 h, and the spectrometric measurements and in vitro pepsin digestion were performed. Increased heating temperature caused the exposure of aromatic residues and an elevation of intensity of synchronous fluorescence spectra, but a reduction in the conformational stability of type I collagen (P < 0.05). Under the in vitro pepsin digestion, the Km value of enzymatic reaction increased as heating temperature rose, but overheating attenuated the affinity of type I collagen to pepsin. Heating at 70 °C for 0.5 h is good for type I collagen to get higher digestion.

Keywords: Digestibility; Heating; Km value; Secondary structure; Type I collagen.

Publication types

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

MeSH terms

Animals
Cattle
Collagen Type I / chemistry*
Digestion
Heating*
Meat / analysis*
Meat Proteins / chemistry*
Models, Molecular
Protein Conformation
Spectroscopy, Fourier Transform Infrared

Substances

Collagen Type I
Meat Proteins