Journal of Agricultural and Food Chemistry · 1997 · 45 citations · 10 references
Life SciencesBiochemistryBiotechnologyGlycobiologyLyophilizationProtein BiochemistryGlobular ProteinsProtein AnalysisProtein GlycoengineeringProtein GlycosylationProtein LyophilizationProtein QualityIonic StrengthIonic Strength DependenceMyofibrillar ProteinsProtein SolubilityProtein Solubility AnalysisProtein Solubility ChangesSolubility
Carp myofibrillar proteins were glycosylated with glucose through the Maillard reaction (the early stage), and their solubility in various ionic strength media was investigated. To react with glucose, lyophilized myofibrils mixed with glucose (at weight ratio of 1:9) were kept at 40 °C and 65% relative humidity for 0−48 h. By glycosylation, myosin and actin became solubilized in low ionic strength media. The total solubility of myofibrillar proteins in 0.01−0.16 M NaCl increased with the progress of glycosylation and was almost equal to the solubility of 0.5 M NaCl. When 17% lysine residue in myofibrillar proteins was reacted with glucose, 61% myosin and 82% actin were solubilized in 0.1 M NaCl. These results indicate that water-soluble myofibrillar proteins can be prepared by glycosylation with the Maillard reaction. Keywords: Fish; myofibrillar proteins; neoglycoprotein; glycosylation; Maillard reaction; solubility
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations