Rheological behavior, conformational changes and interactions of water-soluble myofibrillar protein during heating. (April 2018)

• Record Type: Journal Article
• Authors: Chen, Xing; Xu, Xinglian; Liu, Dongmei; Zhou, Guanghong; Han, Minyi; Wang, Peng
• Is Part Of: Food hydrocolloids. Volume 77(2018)
• Page Start: 524
• Page End: 533
• Publication Date: 2018-04
• Subjects: Water-soluble myofibrillar protein -- Myosin -- High-pressure homogenization -- Thermal stability -- Protein aggregation; Hydrocolloids -- Periodicals; Food additives -- Periodicals; Colloïdes -- Périodiques; Aliments -- Additifs -- Périodiques; Colloids; Food additives; Periodicals; Electronic journals; 664.06
• DOI: 10.1016/j.foodhyd.2017.10.030
• Languages: English
• ISSNs: 0268-005X

Abstract

Abstract: For greater utilization of meat as a source of high-quality protein supplements, we investigated the effects of heating (30–80 °C) on the solubility, rheological behavior, conformational changes and interactions of water-soluble chicken breast myofibrillar protein (WSMP) prepared by high-pressure homogenization (HPH) in comparison with those of salt-soluble myofibrillar protein (SSMP) and HPH-treated SSMP (H-SSMP). Upon heating above 40 °C, WSMP exhibited a shear-thinning behavior with relatively high solubility and flow ability. The thermal gelling ability appeared to be impaired, probably due to weak myosin-head aggregation (30–50 °C) and less interaction between myosin tails (70 °C). WSMP was less prone to unfolding during heating and resulted in smaller protein aggregates in comparison to SSMP and H-SSMP. Moreover, the lower extent of thermally induced disulfide cross-links and hydrophobic and electrostatic interactions led to improved colloidal stability in WSMP. The enhanced solubility and flow ability of WSMP after heating are beneficial to the development of new meat-based products. Graphical abstract: Image 1 Highlights: Thermal properties of water soluble myofibrillar protein were studied. After heating, the protein remained relatively high solubility and flow ability. Thermal gelling of the protein appeared to be inhibited. Protein was stable upon heating, resulting in less protein aggregation. Weak disulfide bonding and hydrophobic interaction led to low protein aggregation.