Abstract
The effect of ovomucoid on gelation of β-lactoglobulin—as induced by heating and subsequent cooling—was investigated using a mixture of 5 % (w/v) ovomucoid/5 % (w/v) β-lactoglobulin and pure β-lactoglobulin solutions (5 and 10 % (w/v)) with subsequent analysis by rheological measurement, ultrasonic spectroscopy, scanning electron microscopy, and sodium dodecyl sulfate polyacrylamide electrophoresis. For the three systems, the dynamic modulus of the mixed-protein sample was smaller than that of either of the two pure β-lactoglobulin samples. Although ultrasonic-relative velocity temperature sweeps for all samples showed that the relative velocities decreased with increasing temperature, the gradient values differed. Namely, the decrease for the mixed-protein sample (12 m/s) was intermediate between those of the pure β-lactoglobulin systems. Ultrasonic attenuations of all samples increased with increasing temperature, and the absolute attenuation value of the mixed-protein sample was also intermediate between those of the two pure β-lactoglobulin samples. Electrophoresis performed with or without 2-mercaptoethanol suggested that ovomucoid forms an aggregate with β-lactoglobulin via intermolecular disulfide bonds. Together, these results suggest that ovomucoid has a synergistic effect on β-lactoglobulin gelation despite the great heat stability.
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Acknowledgments
This study was partly supported by a Grant-in Aid for Scientific Research in Priority Areas (nr 25350116) of Ministry of Education, Science and Culture of Japan. We thank Professor H. Ohta of Tokyo Institute of Technology, Japan, for the helpful suggestion and discussion.
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Yuno-Ohta, N., Kato, T., Ashizawa, S. et al. Role of ovomucoid in the gelation of a β-lactoglobulin-ovomucoid mixture. Colloid Polym Sci 294, 1065–1073 (2016). https://doi.org/10.1007/s00396-016-3864-0
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DOI: https://doi.org/10.1007/s00396-016-3864-0