High-pressure effects on the molecular aggregation and physicochemical properties of myosin in relation to heat gelation.
Food Res Int
; 99(Pt 1): 413-418, 2017 09.
Article
em En
| MEDLINE
| ID: mdl-28784500
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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Alimentares
/
Miosinas
/
Músculos Psoas
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Manipulação de Alimentos
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Carne
Limite:
Animals
Idioma:
En
Revista:
Food Res Int
Ano de publicação:
2017
Tipo de documento:
Article