AI Article Synopsis
- - The study compared the thermal, rheological (flow) and microstructural properties of myosin at different concentrations with mixtures of myosin and heat-denatured or native beta-lactoglobulin in specific salt and buffer conditions.
- - It was found that both myosin and the myosin/heat-denatured beta-lactoglobulin mixtures had similar thermal denaturation patterns, but the mixed system displayed an extra endothermic peak during heating.
- - The gelling behavior revealed that myosin and myosin/HDLG formed stronger gels with higher storage moduli compared to myosin/beta-LG, and as the pH decreased, both gel points and storage moduli increased, showing that HDLG was
Article Abstract
Thermal, rheological, and microstructural properties of myosin (1 and 2% protein) were compared to mixtures of 1% myosin and 1% heat-denatured beta-lactoglobulin aggregates (myosin/HDLG) and 1% myosin and 1% native beta-lactoglobulin (myosin/beta-LG) in 0.6 M NaCl and 0.05 M sodium phosphate buffer, pH 6.0, 6.5, and 7.0 during heating to 71 degrees C. Thermal denaturation patterns of myosin and myosin/HDLG were similar except for the appearance of an endothermic peak at 54-56 degrees C in the mixed system. At pH 7.0, 2% myosin began to gel at 48 degrees C and had a storage modulus (G') of 500 Pa upon cooling. Myosin/HDLG (2% total protein) had a gel point of 48 degrees C and a G' of 650 Pa, whereas myosin/beta-LG had a gel point of 49 degrees C but the G' was lower (180 Pa). As the pH was decreased, the gel points of myosin and myosin/HDLG decreased and the G' after cooling increased. The HDLG was incorporated within the myosin gel network, whereas beta-LG remained soluble.
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| http://dx.doi.org/10.1021/jf020413e | DOI Listing |
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