TRANSGLUTAMINASE MEDIATED POLYMERIZATION OF CRUDE ACTOMYOSIN REFINED FROM MECHANICALLY DEBONED POULTRY MEAT¹²

Abstract

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.

Modification of functional quality of raw myofibril preparation obtained from water-washed mechanically recovered chicken meat

“…Results obtained from electrophoretic analysis for myofibril preparation subjected to the action of the enzyme are similar to those reported previously by other authors [10,31,32]. Proteins of comminuted chicken breast muscle with an addition of TG incubated at 40°C were characterised by a lower intensity of MHC and troponin T with an extension of incubation time (Fig.…”

“…No changes were observed in the actin band [31]. Similar changes in relation to myosin were earlier found in case of MRPM [32]. In contrast, no changes were found in the content of actin obtained from beef [10], chicken meat [31] and fish [33].…”

Enzymatic modification of protein preparation obtained from water-washed mechanically recovered poultry meat

“…Mammalian species, such as beef, pork and whale, are classified as nonsetting species (Niwa, Yamada, Kanoh, & Nakayama, 1989). However, Akamittath and Ball (1990) reported that setting was induced in crude actomyosin from turkey at 4 and 37 1C with the aid of guinea pig liver TG. Kim, Carpenter, Lanier, and Wicker (1993) reported that polymerization of beef actomyosin was induced by an addition of TG.…”

“…Since covalent bonds possess high binding energy and the ability to crosslink muscle proteins, it is believed to be an important process in building structure in muscle foods; therefore, it is reasonable to speculate that such crosslinks in refined surimiprocessed MRPM will impart improved binding and textural attributes in restructured meat products (Akamittath & Ball, 1992).…”

Quality attributes and consumer acceptance of new ready-to-eat frozen restructured chicken

“…As the objective of this study was to obtain restructured products with texture characteristics similar to those of a chicken fillet, the results showed that addition of the TG enzyme refined the MSCM by cross-linking actomyosin (Akamittath and Ball 1992). This result corroborated the results described by Keeton (2001), who reported that TG influences the texture of meat products, and these authors also stated that TG is used to improve the rheological properties of food and can be applied in combination with other ingredients, such as salt, phosphates and alkali curing.…”