Improvement of the physical properties of pepsin-solubilized elastin-collagen film by crosslinking.
Pepsin-solubilized elastin (PSE)-conjugated collagen film was prepared from a collagen matrix with PSE by drying it and crosslinking the constituents with water-soluble carbodiimide or microbial transglutaminase to improve the physical properties of the collagen film. The crosslinking reduced the solubility and improved the thermal stability, the thermal transition properties, and the elasticity of the control film in water. In particular, water-soluble carbodiimide strongly influenced these properties. The PSE-conjugated collagen film showed good permeation by water-soluble tasting substances such as oligosaccharides and amino acids, but poor permeation by polysaccharide, protein, and hydrophobic substances such as retinol and cholesterol.
Takahashi
K
K
Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Japan. k-taka@cc.tuat.ac.jp
Nakata
Y
Y
Someya
K
K
Hattori
M
M
D002152:Calorimetry, Differential Scanning; D003094:Collagen / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000378:metabolism; D004549:Elastin / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning; D010434:Pepsin A / Q000378:metabolism*; D010539:Permeability; D012995:Solubility; D011503:Transglutaminases / Q000378:metabolism
D003432:Cross-Linking Reagents; D003094:Collagen; D004549:Elastin; D011503:Transglutaminases; D010434:Pepsin A