l-Arginine and l-lysine retard aggregation and polar residue modifications of myofibrillar proteins: Their roles in solubility of myofibrillar proteins in frozen porcine Longissimus lumborum

Use of basic amino acids to improve gel properties of PSE‐like chicken meat proteins isolated via ultrasound‐assisted alkaline extraction

“…l ‐His/ l ‐Arg/ l ‐Lys had relatively high isoelectric points. They tended to interact with the negatively charged protein residues on PPI primarily via electrostatic effect, which contributed to expose more sites of proteins to bind water and suppress protein aggregation (Bao et al., 2022; Fu et al., 2017).…”

“…Basic amino acids inhibited PPI aggregation and changed the secondary structure, resulting in a low α‐helix content and high PPI solubility (Figure 5; Table 1). Basic amino acids increased the PPI cross‐linking during heat‐induced gelation and form a tight gel network structure (Bao et al., 2022; Javith et al., 2022). PPI gel with a homogeneous and fine structure exhibited high gel strength (Figures 1 and 4) and trapped more water, resulting in low cooking loss, as shown in the above results (Figures 2 and 3).…”

“…(2020) reported that the addition of l ‐Arg decreases the proportion of α‐helix and increases the proportion of other protein secondary structures in the bighead carp ( Aristichthys nobilis ) myosin gel. l ‐Arg/ l ‐Lys enhances the electrostatic repulsion between MPs and promotes the stretching of molecular chains, leading to the reduction in the content of α‐helix and increase in β‐sheet (Bao et al., 2022; Wu et al., 2023). The α‐helix‐to‐β‐sheet conversion has a significant effect on heat‐induced protein gel (Jiang et al., 2023).…”

Quality improvement of prerigor salted ground chicken breast with basic amino acids at low NaCl level

“…In recent years, basic amino acids (arginine, lysine, and histidine) were reported to exhibit the capacity to improve functional properties (protein solubility, secondary structure, emulsion and gel characteristics) of myofibrillar protein, myosin or bologna-type sausages when the NaCl content was reduced ( Gao et al, 2019 ; da Silva et al, 2020 ; Shi et al, 2020 ; Guo et al, 2021 ; Bao et al, 2022 ). The electrostatic interactions between basic amino acids and myosin were thought to be the main cause ( Li et al, 2019 ; Shi et al, 2021 ).…”

l‐Arginine and l‐lysine can weaken the intermolecular interactions of main myofibrillar proteins: the roles in improving the tenderness of pork Longissimus lumborum muscle

“…In recent years, some studies have demonstrated that exogenous basic amino acids can effectively improve the quality and sensory attributes of ham, dry‐cured loin, dry‐salted grass carp, cured and cooked loin, sausages and refrigerated prepared pork chops, as well as maintain the solubility to enhance the hydration characteristics of frozen pork myofibrillar proteins, and the gel properties of duck myofibrillar proteins during freeze–thaw cycles (Bao et al ., 2021, 2022; Chen et al ., 2022; Zhang et al ., 2022; Li et al ., 2023). Among these amino acids, l ‐arginine (Arg) and l ‐lysine (Lys) have been confirmed to enhance water holding capacity of meat and meat products, improve their colour and tenderness (Zhu et al ., 2018; Bao et al ., 2021) and inhibit the oxidation of their protein and fat (Zhang et al ., 2021).…”