Antioxidative Ability of Chicken Myofibrillar Protein Developed by Glycosylation and Changes in the Solubility and Thermal Stability

Random-centroid Optimization Reveals the Strongest Superoxide Anion Radical Scavenging Activity of Maltose- and Ribose-conjugated Chicken Myofibrillar Protein

“…3. Native chicken Mfs hardly demonstrated SOSA in the range of 2.0-6.0 mg of protein/mL, in agreement with our earlier studies focusing on glycated chicken Mfs with maltose (Nishimura et al, 2011b; 59 38 37 . 9 5 .…”

“…ESR Spectroscopy ESR spectroscopy was carried out with an X-band ESR spectrometer (JES-FA 100; Jeol Datum Ltd., Tokyo, Japan) at room temperature in a 0.4-mm flat cell (ES-LC 12; Jeol Datum Ltd.), according to the previously published method (Nishimura et al, 2011b). Manganese was used as an internal standard.…”

“…Functional alterations to the Maillard reaction can result from glycation of chicken myofibrillar proteins (Mfs) with sugars (Nishimura et al, 2011a,b;Isono et al, 2012;Nishimura et al, 2015;Nishimura and Saeki, 2016). Glycation with maltose confers improved solubility in a low ionic strength medium, higher thermal stability (Nishimura et al, 2011a,b) and antioxidant abilities (Nishimura et al, 2011b), as measured by superoxide anion radical (O _ 2 ) scavenging activities (SOSA). Antioxidant ability is attributed to the primary structure-the specific peptide sequence of the glycated chicken Mfsirrespective of the protein shape (Isono et al, 2012).…”

Improved gelation functionalities of myofibrillar protein from pale, soft and exudative chicken breast meat by nonenzymatic glycation with glucosamine

“…() have confirmed that the solubilities of chicken myofibrillar protein (MP) and chicken actomyosin were improved after glycation. In addition, the emulsifications formed by the Silver Carp protein (You et al ., ) and the thermal stability of chicken MP (Nishimura et al ., ) were also improved with glycation.…”

A comparative study of physicochemical and functional properties of silver carp myofibrillar protein glycated with glucose and maltodextrin

“…4 Glycation is an effective method to improve the functional properties of sh proteins and even endows them with a novel functionality. 5 The impact of glycation through the Maillard reaction on food proteins has been widely reported, such as improving the emulsifying properties of sh Mf glycated with alginate oligosaccharides, 6 raising the solubility of carp Mf conjugated with ribose, 7 increasing the heat stability of carp Mf glycated with dextran, 8 enhancing the antioxidant effect of chicken Mf reacted with glucose and maltose, 9 and improving the gel properties by glycation with konjac glucomannan. 10 However, these research efforts paid less attention to the impact of the structure and molecular weight of saccharides, and the understanding of the relationships between the types of saccharides and functional properties of glycated Mf is seldom reported.…”