Gel-Forming Ability of Glycated Chicken Myofibrillar Proteins with Enhanced Antioxidant Properties

Abstract

  Chicken myofibrillar proteins (Mfs) glycated with maltose formed a rigid gel when heated for up to 240 min at 90°C. This gel was more rigid than that produced from natural or unmodified chicken Mfs that were prepared without maltose, under the same heating conditions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that disulfide bonding occurred during the first half of the heating period and subsequent polymer formation with cross-linking occurred in the second half. Moreover, glycation of chicken Mfs with maltose was more rapid during the gelation process. Observation of the microstructures under a cryo-scanning electron microscope revealed that the fibers in the gel structure prepared from chicken Mfs glycated with maltose were thicker than those in the gel structure prepared from natural or unmodified chicken Mfs and that a network structure was developed that led to the formation of a more rigid gel.