Changes in Solubility and Thermal Stability of Chicken Myofibrillar Protein by Glycosylation

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

“…These results indicate that the thermal stability of chicken myofibrillar proteins had been improved by conjugating with maltose and that the mixing ratio of 1:4 of myofibrillar proteins to maltose was enough to acquire thermal stability in 0.1 and 0.5 M NaCl. Although this improvement in the thermal stability of myofibrillar protein was also observed after a 6-h reaction, 33) this might be attributable to the suppressed thermal aggregation of myosin by the attaching sugars and the increasing hydration with water due to the presence of a large enough amount of the hydroxy group.…”

“…The glycosylation of chicken myofibrillar protein with glucose and maltose by the 6-h incubation at 60 C and 35% RH brought about an improvement in both the solubility and thermal stability. 33) However, such other functional properties as SOSA did not develop (data not shown). Since Maillard reaction intermediates accumulated and the possible development of new functional properties could be expected, the reaction was then extended in time so that the solubility was not markedly decreased.…”

“…The amount of available lysine in this product was about 40%, suggesting that about 120 molecules of maltose were conjugated with the myosin heavy chain, since about 200 residues of lysine are present in one molecule. 33) The total number of hydroxy groups accordingly became 960 for each myosin heavy chain, and solubility was improved by increased hydration. This improved solubility would have resulted from the dissociation between myosin and actin, as well as from the loss of filament-forming ability of the myosin rods by glycosylation.…”

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

“…Protein is known to be stabilized in the presence of saccharide. 30 As reported by Nishimura et al, 14 the difference in protein solubility with a decrease seemed to be caused by a shortage of saccharide as a thermal protectant. In this study, saccharides were only two times the weight of protein, which might be too small to defend Mf.…”

Preparation of Chicken Myofibrillar Protein-Maltose Conjugate Having Multi-Food Functions Using Random-Centroid Optimization

“…Moreover, using a comparatively small amount of sugar brings about the same functional alterations to chicken Mfs, such as rising solubility in a low ionic strength medium and higher thermal stability (Nishimura et al, 2011a,b). Furthermore, we found that the Maillard reaction with maltose confers antioxidant abilities on chicken Mfs (Nishimura et al, 2011b). This antioxidant ability is attributed to the primary structure or specific peptide sequence of the glycated chicken Mfs, irrespective of the protein shape (Isono et al, 2012).…”