|
In order to elucidate texturization mechanism of extrudated protein, egg white lysozyme was heated under high pressure conditions, and its solubility and changes of molecular weight were investigated. Under high pressure conditions of 100, 300 and 600 kg/㎠, solubility decreased gradually with increasing temperature in the samples heated at 70, 120 and 150 ℃ and decreased notably with increasing pressure at 200 ℃. Polymerization was found in the samples heated at 150 and 200 ℃ while a band which located below monomer(low-molecular) could be recognized. Molecular weight of the low-molecular was estimated to be about 6,000∼9,000 and no smaller peptide was recognized. The polymerization may have occured by disulfide crosslinking in the samples heated at 120℃ but other crosslinking may have played a role in those at 150 and 200℃.
|