Solubility improvement of shellfish muscle proteins by reaction with glucose and its soluble state in low-ionic-strength medium.
When myofibrillar proteins of scallop striated adductor muscle were reacted with glucose through the Maillard reaction, the change in the solubility of myofibrillar proteins in 0.05-0.5 M NaCl solutions during glycosylation and their soluble states were investigated. The solubility in low-ionic-strength media increased greatly with the progress of the Maillard reaction. The solubility in 0.1 M NaCl reached 83% when more than 60% of lysine residues in myofibrillar proteins were modified by glucose. However, the excess progress of the Maillard reaction impaired the improved solubility of myofibrillar proteins in a low-ionic-strength medium. Myosin, actin, and paramyosin in glycosylated myofibrillar proteins were solubilized independently regardless of NaCl concentration. In addition, the glycosylated myosin lost its filament-forming ability and existed as a monomer in 0.1 M NaCl.
Katayama
Shigeru
S
Graduate School of Fisheries Sciences, Hokkaido University, Minato 3, Hakodate, Hokkaido 041-8611, Japan.
Shima
Junji
J
Saeki
Hiroki
H
D000199:Actins / Q000737:chemistry; D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005947:Glucose / Q000737:chemistry*; D006031:Glycosylation; D015416:Maillard Reaction; D008974:Mollusca; D009124:Muscle Proteins / Q000737:chemistry*; D009210:Myofibrils / Q000737:chemistry; D009218:Myosins / Q000737:chemistry; D009994:Osmolar Concentration; D012758:Shellfish; D012965:Sodium Chloride / Q000494:pharmacology; D012995:Solubility; D014335:Tropomyosin / Q000737:chemistry
D000199:Actins; D009124:Muscle Proteins; D014335:Tropomyosin; D012965:Sodium Chloride; D009218:Myosins; D005947:Glucose