Cross-linking and gel formation of water-soluble lysine polypeptides. An insolubilization model reaction for adhesive proteins.
Insolubilizing studies of water-soluble synthetic polypeptides containing lysine residues were examined using organic aliphatic and aromatic cross-linking agents such as dialdehydes, diacyl chlorides and diactive ester, together with an enzyme tyrosinase, in water and simulated seawater systems. The cross-linking reaction was characterized by the viscosity and turbidity changes. Among the organic cross-linking agents used aliphatic glutaraldehyde and aromatic o-phthalaldehyde were the most effective. When excess organic cross-linking agents were added to the lysine polypeptide systems, the corresponding solid gels were formed. As a whole, the molecular weight of the samples, the amino acid compositions, the cross-linking agent used, the molar ratios between cross-linking agents and functional residues and system pH were found to have roles in the insolubilizing reaction and the gel formation. The cross-linking results obtained were compared with those of the polypeptide-tyrosinase systems, whose deep brownish red colour was decolorized by the addition of L-ascorbic acid.
Yamamoto
H
H
Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Ueda, Japan.
Tanisho
H
H
Ohara
S
S
Nishida
A
A
D005782:Gels; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine / Q000737:chemistry*; D046911:Macromolecular Substances; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry*; D012995:Solubility; D014783:Viscosity; D014867:Water
D005782:Gels; D046911:Macromolecular Substances; D010455:Peptides; D014867:Water; D008239:Lysine