|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|5768114||1413213||2017||6 صفحه PDF||سفارش دهید||دانلود رایگان|
- Myosin subjected to high-pressure (HP) treatment (â¥Â 200Â MPa) had lower solubility.
- Pressure intensities of 200Â MPa and above induced dimerization of myosin molecules.
- Morphologically swollen myosin was observed following HP treatments at 200 & 300Â MPa.
- Samples treated at 200 and 300Â MPa HP conditions had improved shear-thinning behaviors.
- Relationship between myosin molecular traits and gelation functionalities were proposed.
Myosin was extracted from the M. psoas muscle of rabbits, and dissolved in 0.6Â M KCl buffer (pHÂ 6.5). Effects of high-pressure (HP, 100 to 300Â MPa, 9Â min, 25Â Â°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 200Â MPa HP treatment had lower solubility than samples treated at other pressures (PÂ <Â 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 (10Â mg/mL) was improved by HP treatment (â¥Â 200Â MPa), 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 â¥Â 200Â MPa.
Journal: Food Research International - Volume 99, Part 1, September 2017, Pages 413-418