Oxidation of purified bovine myoglobin: effects of pH, sodium chloride, sodium tripolyphosphate, and binders

Sous-vide cooking as a practical strategy to improve quality attributes and shelf stability of reduced-salt chicken breast ham

“…However, it has been well known that the adding sodium chloride is one of the factors accelerating the oxidation of biological molecules in meat products ( Ladikos and Lougovois, 1990 ). Chen et al (1992) have found that an increase in sodium chloride concentration (0–1.5%) could accelerate myoglobin oxidation, causing metmyoglobin formation. Unlike the unsalted condition of previous studies, thus, the sodium chloride salting process performed in this study might be one of the reasons affecting the color change in sous-vide cooked chicken breast.…”

Textural Properties and Color Characteristics of Restructured Beef Steaks With Selected Binders and Nomeat Adjuncts

“…A possible explanation for the enhanced stability in restructured steaks made with CME (HSP) may be the result of a slightly higher pH for steaks containing CME (pH 5.99) than the restructured control with NaCl/STP (pH 5.83). In previous studies using purified bovine myoglobin solutions, this elevation in pH due to CME was not effective in decreasing metmyoglobin when compared to control solutions (Chen et al 1992). Therefore, the increased stability within a meat system may be the result of an interaction between the meat and CME.…”

Quantitation of heme proteins from spectra of mixtures

“…This method can be applicable in food chemistry and in the biochemistry of meat pigments. The studies of Chow (1991) and Chen et al (1992) are examples. This method is applicable to investigations of oxidative damage to animal tissues by toxic oxidants (Chen, 1993a).…”