ABSTRACT
Physical properties of shark gelatin were examined during gel formation and postgelation in comparison with pig gelatin. Samples with various concentrations and pH values were evaluated by breaking strength, dynamic viscoelasticity, and dynamic light scattering. Sol-gel and gel-sol transition temperatures for shark gelatin were remarkably lower than those for pig gelatin. Shark gelatin gel shows a narrower pH range to form a stable gel compared with pig gelatin. Melting enthalpy of shark gelatin gel was greater than that of pig gelatin gel, and G' of shark gelatin gel changed more extensively with rising temperature in comparison with pig gelatin gel. It is concluded that shark gelatin has different characteristics from pig gelatin not only for gel characteristics but also for the solution property.
Subject(s)
Gelatin/chemistry , Animals , Elasticity , Gels , Sharks , Skin/chemistry , Swine , Thermodynamics , ViscosityABSTRACT
Alkali-solubilized collagens, prepared by alkali-acid extraction and alkali direct extraction (abbreviated AASC and ALSC, respectively), were characterized by dynamic viscoelastic measurement of collagen solution (10 mg/mL). The optimum preparative conditions in terms of yield and polypeptide size are as follows: for the alkali-acid extraction, a pretreatment with 0.5 or 1 M NaOH containing 15% Na(2)SO(4) within 5 days at 20 degrees C followed by the subsequent acid extraction, and for the alkaline direct extraction, a treatment with 0.5 M NaOH containing 10% NaCl at 4 degrees C for 20-30 days. A major portion of the polypeptide sizes of AASC and ALSC is composed of alpha chains (alpha1 and alpha2). Dynamic viscoelasticity of collagen solution was measured as a function of temperature. AASC showed a greater contribution of elastic behavior rather than viscous behavior. On the contrary, ALSC exhibits a stronger viscous behavior than elastic behavior.