|
KMID : 0380619870190020089
|
|
Korean Journal of Food Science and Technology
1987 Volume.19 No. 2 p.89 ~ p.96
|
|
|
Changes of Hydrophobicity , Solubility , SH Group and Protein - Protein Interaction in Yellowtail Myosin and Whelk Paramyosin During Thermal Denaturation
|
|
|
|
|
Abstract
|
|
|
|
The denaturation mechanism of the protein during heating of myosin and paramyosin extracted from the ordinary muscle of yellowtail (Seriola qrinqueradits) and the adductor muscle of whelk (Neptunea arthritica cuming) were investigated by analyzing the hydrophobicity, solubility, SH group and protein-protein interaction. The free hydrophobic residue of the two proteins were increased by increase of heating temperature up to 65℃ and then decreased for further temperature raise. The protein-protein interaction was proportional to the increment of the free hydrophobic residue. The aggregation of protein was begun from 65℃ with the decrease of the free hydrophobic residues. The results of Arrhenius equation for the data on proteinprotein interaction showed that the denaturation course was made up with multi-steps in the myosin and two-steps in the paramyosin. The number of free hydrophobic residue and SH group, solubility and protein-protein interaction were significantly differed with the denaturation temperature (p$lt;0.01).
|
|
|
KEYWORD
|
|
|
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|