Physicochemical, conformational and functional properties of silver carp myosin glycated with konjac oligo-glucomannan: Implications for structure-function relationships

Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix)

“…3,4 To help overcome these disadvantages, exogenous substances such as polysaccharides may be added to improve gel-forming capacity and gel properties. [5][6][7] Konjac glucomannan (KGM), as a water-soluble neutral polysaccharide, is derived from konjac tubers. 8,9 It is widely believed that the acetyl group is closely related to the properties of KGM, such as its gelling and thickening properties.…”

“…16 Liu et al (2017) suggested that konjac oligoglucomannan (KOG) had a positive effect on the conformational and functional properties of myosin. 7 The deacetylation of KGM tempered changes in protein structure, and strengthened the gel network under high temperature (120 C) treatment. 17 Liu et al (2019a; 2019b) studied the deacetylation of konjac oligo-glucomannan on the physico-chemical and structural properties of silver carp myosin as well.…”

Effects of Enzymatic Konjac Glucomannan Hydrolysates on Textural Properties, Microstructure, and Water Distribution of Grass Carp Surimi Gels

“…The influence of KEH on the structure and water distribution of surimi gels was mostly depending on the molecular weight of KGM. KEH with large M w tended to self-aggregate in surimi gels as being unlikely to be fully extend, while those with low M w might preferred to be well extended rather than easy-to-bind water molecules or interact with proteins [ 40 ]. It was speculated that there were two possible methods to enhance the gel strength of surimi by the addition of high M w KEH (K1 and K2): on the one hand, the water absorption of KEH caused the protein concentration in the matrix and, thus, led to an increase in α-helix structure in surimi protein ( Figure 2 ); on the other hand, the aggregates of KGM hydrolysate physically filled the network of surimi ( Figure 2 ) and improved the gel properties of surimi [ 41 ].…”

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

“…The observed altered functionality is possibly due to steric hindrance and the negative impact on filament formation from ε‐amino residues of lysine (Nishimura et al., 2011). Neoglycoprotein glycated with maltose exhibited superior solubility and heat stability compared to glucose because of its higher molecular weight (Liu, Luo, et al., 2017). Furthermore, a five‐member ring monosaccharide, such as ribose, was suggested to react faster than a six‐member ring, such as maltose, because it requires a lower temperature and shorter time for ribose to reach the highest level of glycation compared to maltose (Nishimura & Saeki, 2018).…”