High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution

Xing Chen; Youling L Xiong; Xinglian Xu

doi:10.1016/j.foodchem.2019.01.131

High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution

Food Chem. 2019 Jul 1:285:31-38. doi: 10.1016/j.foodchem.2019.01.131. Epub 2019 Jan 31.

Authors

Xing Chen¹, Youling L Xiong², Xinglian Xu³

Affiliations

¹ State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Key Laboratory of Meat Processing and Quality Control, Ministry of Education and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China. Electronic address: xingchen@jiangnan.edu.cn.
² State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, United States. Electronic address: ylxiong@uky.edu.
³ Key Laboratory of Meat Processing and Quality Control, Ministry of Education and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China. Electronic address: xlxus@njau.edu.cn.

PMID: 30797350
DOI: 10.1016/j.foodchem.2019.01.131

Abstract

This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (H₂O₂, at 0, 40, 80, 160 and 320 μmol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 °C for 10 min) in aqueous solution. The addition of H₂O₂ blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H₂O₂ by disrupting the intact myofibril structure and exposing buried -SH groups, and this resultedin stronger inhibition of thermal aggregation therefore improved solubility of MP. More than 75% of heated MP remained soluble after the treatment with HPH and 160 μmol/g H₂O₂, while untreated samples formed a gel upon heating. These results proved that HPH combined with H₂O₂ is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.

Keywords: Heat stability; High-pressure homogenization; Hydrogen peroxide; Myofibrillar protein; Protein beverage; Sulfhydryl blockage.

MeSH terms

Animals
Chickens / metabolism*
Hot Temperature
Hydrogen Peroxide / chemistry*
Muscle Proteins / chemistry
Muscle Proteins / metabolism*
Myofibrils / metabolism*
Particle Size
Pressure
Protein Stability
Rheology
Solubility
Sulfhydryl Compounds / chemistry*
Water / chemistry

Substances

Muscle Proteins
Sulfhydryl Compounds
Water
Hydrogen Peroxide