High-pressure effects on the molecular aggregation and physicochemical properties of myosin in relation to heat gelation

Siwen Xue; Huijuan Yang; Huhu Wang; Alexander Atuya Tendu; Yun Bai; Xinglian Xu; Hanjun Ma; Guanghong Zhou

doi:10.1016/j.foodres.2017.06.014

High-pressure effects on the molecular aggregation and physicochemical properties of myosin in relation to heat gelation

Food Res Int. 2017 Sep;99(Pt 1):413-418. doi: 10.1016/j.foodres.2017.06.014. Epub 2017 Jun 3.

Authors

Siwen Xue¹, Huijuan Yang², Huhu Wang², Alexander Atuya Tendu³, Yun Bai², Xinglian Xu⁴, Hanjun Ma⁵, Guanghong Zhou²

Affiliations

¹ Key Laboratory of Meat Products Processing, Ministry of Agriculture, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, PR China.
² Key Laboratory of Meat Products Processing, Ministry of Agriculture, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China.
³ College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, PR China.
⁴ Key Laboratory of Meat Products Processing, Ministry of Agriculture, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China. Electronic address: xlxus@njau.edu.cn.
⁵ School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, PR China. Electronic address: hjma@hist.edu.cn.

PMID: 28784500
DOI: 10.1016/j.foodres.2017.06.014

Abstract

Myosin was extracted from the M. psoas muscle of rabbits, and dissolved in 0.6M KCl buffer (pH6.5). Effects of high-pressure (HP, 100 to 300MPa, 9min, 25°C) treatment on myosin solubility, molecular traits (molecular weight and morphology), flow behavior and strength of heat-induced myosin gels were studied and compared with the untreated controls. Myosin subjected to 200MPa HP treatment had lower solubility than samples treated at other pressures (P<0.05). Molecular dimerization and morphological swelling of myosin was observed using gel-permeation chromatography and atomic-force microscopy. Additionally, the shear-thinning behavior of myosin solutions (10mg/mL) was improved by HP treatment (≥200MPa), and a positive trend in gel-strength enhancement was inferred. It is postulated that significant morphological changes in myosin accounted for changes in its functional properties, by the influence of HP treatment on protein-protein and/or protein-water interactions. There is a relationship between molecular morphology and the coalescing behavior of myosin, since significant changes of both attributes were observed at pressures ≥200MPa.

Keywords: Dimerization; Functional properties; High-pressure processing; Mechanism; Molecular morphology; Myosin.

Publication types

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

MeSH terms

Animals
Chromatography, Gel
Dietary Proteins / chemistry*
Food Handling / methods*
Gels
Male
Meat*
Microscopy, Atomic Force
Molecular Weight
Myosins / chemistry*
Pressure
Protein Conformation
Protein Multimerization
Psoas Muscles / chemistry*
Rabbits
Rheology
Solubility

Substances

Dietary Proteins
Gels
Myosins