TRANSGLUTAMINASE MEDIATED POLYMERIZATION OF CRUDE ACTOMYOSIN REFINED FROM MECHANICALLY DEBONED POULTRY MEAT2

Autor:	Joseph G. Akamittath, Hershell R. Ball
Rok vydání:	1992
Předmět:	chemistry.chemical_classification biology Tissue transglutaminase technology industry and agriculture macromolecular substances Polymer Positive correlation Catalysis chemistry.chemical_compound Monomer chemistry Polymerization Covalent bond Myosin Polymer chemistry biology.protein Food Science
Zdroj:	Journal of Muscle Foods. 3:1-14
ISSN:	1745-4573 1046-0756
DOI:	10.1111/j.1745-4573.1992.tb00666.x
Popis:	Transglutaminase catalyzed crosslinking was initiated in crude actomyosin (refined from surimi processed, mechanically deboned turkey meat – MDTM) at 37°C and 4°C and pH 6.0 and 7.0. Crosslinked reaction products which were analyzed by SDS-PAGE, indicated a 60% decrease in myosin monomers and a 25% increase in myosin polymers. Polymerization was favored at 37°C. At 37°C, pH did not appear to affect the crosslinking process. However, at 4°C, crosslinking appeared to be enhanced at pH 6.0 over that at pH 7.0. A positive correlation (r = 0.99 and 0.95) was exhibited between the percentage decrease in free amino groups and the decrease in myosin monomer content. Results indicate that guinea pig liver transglutaminase can be utilized to introduce covalent crosslinks in crude actomyosin refined from MDPM.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::277b9b74d4c1f8eabd95299c8ce6faea https://doi.org/10.1111/j.1745-4573.1992.tb00666.x Zobrazit plný text záznamu Plný text