The Solubility and Structures of Porcine Myofibrillar Proteins under Low-Salt Processing Conditions as Affected by the Presence of <span style="font-variant: small-caps">L</span>-Lysine

Abstract

This study aimed to investigate the presence of L-lysine (Lys) on the solubility and structures of myofibrillar proteins (MFPs) at different ionic strengths. Porcine MFPs were incubated at 4 °C with various levels of ionic strengths (0.15, 0.3, or 0.6 M NaCl) with or without the presence of 20 or 40 mM Lys. After 24 h of incubation, MFP solubility and turbidity were determined, and the particle size distribution, circular dichroism spectra, and intrinsic tryptophan fluorescence of MFP were analyzed to obtain their secondary and tertiary structure. Results showed that the solubilization effects of Lys on MFPs are dependent on the ionic strength. Particularly, the presence of Lys could improve MFP solubility at 0.3 M, which resembles salt-reducing processing conditions. Concomitantly, the secondary and tertiary structures were observed to change as a result of the varying ionic strengths and the addition of Lys, including myofibril swelling, dissociation of myosin filaments, uncoiling of α-helix, and unfolding of the tertiary structure. The possible mechanisms underlying the solubilization effects of Lys on MFPs at low ionic strengths are discussed from the perspective of protein structural changes.

Keywords

• myofibrillar proteins
• L-lysine%22%2C%22default_operator%22%3A%22AND%22%7D%7D%7D"> <span style="font-variant: small-caps">L</span>-lysine
• solubility
• conformation
• low salt