Alpha-chain subunits were separated from tilapia skin gelatin using ultrafiltration, and the physicochemical properties of obtained subunits were investigated. As a result, α1-subunit and α2-subunit could be successfully separated by 100 kDa MWCO regenerated cellulose membranes and 150 kDa MWCO polyethersulfone membranes, respectively. Glycine was the most dominant amino acid in both α1-subunit and α2-subunit.
View Article and Find Full Text PDFThe effect of blend ratio and pH on the physical properties of surimi-gelatin composite films was investigated. Tensile strength (TS), film water solubility and soluble proteins of composite films increased with the increasing proportion of gelatin, while elongation at break (EAB) decreased. The TS of neutral films with the same ratio of surimi and gelatin were lowest, while increased at acidic or alkaline conditions.
View Article and Find Full Text PDFUnlabelled: Edible films from squid mantle muscle plasticized with different plasticizers were stored at 25 °C, 50% RH before the determination of physical properties. The results showed that tensile strength significantly increased (P < 0.05) upon the storage time, especially for the film plasticized with glucose, while there was no significant change (P ≥ 0.
View Article and Find Full Text PDFComp Biochem Physiol B Biochem Mol Biol
June 2003
Trimethylamine-N-oxide demethylase (TMAOase) from lizardfish (Saurida micropectoralis) was partially purified by acidification and diethylaminoethyl (DEAE)-cellulose chromatography. The enzyme was purified 82-fold with a yield of 65.4%.
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