Depolymerization Behavior of Freeze-Thaw Recombinant Glutenin Macropolymer as Influenced by Antifreeze Protein from
Yanjie Zhang1,2,3, Jinhui Wang1,2,3, Yixuan Feng1,2,3
1College of Food Science and Technology, Henan Agricultural University, Zhengzhou 450002, China.
Abstract:
Glutenin and gliadin were mixed at different ratios, with 0.5% Avena sativa antifreeze protein (AsAFP) as the experimental group, and subjected to freeze-thaw cycles. Glutenin macropolymer (GMP) extracted from samples was analyzed for content, free sulfhydryl, secondary structure, and thermal stability. A model between the GMP content and freeze-thaw times was established, followed by correlation analysis. Results showed that the GMP content decreased with increasing gliadin proportion and freeze-thaw cycles, indicating depolymerization. Free sulfhydryl content increased, while α-helix, β-sheet, denaturation temperature, and denaturation enthalpy gradually decreased. Correlation analysis revealed that disulfide bond cleavage was the main cause of GMP depolymerization. This study provides a theoretical basis for AsAFP application in frozen dough and offers insights into optimizing the gluten composition for freeze-thaw stability.
