Add time:08/18/2019         Source:sciencedirect.com

To clarify the gel formation mechanism of isolated proteins recovered from blue round scads by isoelectric solubilization/precipitation, the physiochemical, conformational and gelation properties of the major protein myosin treated by acidic-(AM) or alkaline-(KM) pH-shifting were investigated and compared with native myosin (NM). The solubility in all myosin samples dropped significantly at 40 °C, with remarkable increases of particle size, turbidity and surface hydrophobicity. Among the samples, AM exhibited the lowest solubility and highest turbidity than NM and KM as the temperature was higher than 40 °C, indicating that AM is easily to be denatured and aggregated. Circular dichroism (CD) analysis showed that both acidic and alkaline pH treatments led to conformational changes of myosin, together with α-helix content variations. When pH was readjusted to neutral, KM recovered its structure similar to NM, while AM failed to refold to its native state. NM exhibited the highest storage modulus (G′) at 90 °C, while AM revealed the lowest G′ value. Furthermore, AM did not change obviously during heating, especially at the gelling temperature range (60–90 °C). These results strongly suggested that acidic treatment led to an irreversible conformational change in myosin, consequently induced a fierce denaturation and aggregation at the initial stage of heating, and eventually led to a complete loss of gel-forming ability. Alkaline pH-shifting, on the other hand is thus more feasible for protein recovery from blue round scads.

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