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<p>Ice recrystallization is a major cause of texture and quality deterioration during frozen storage, and antifreeze proteins (AFPs) have attracted attention as potential non-colligative ice-growth inhibitors. This study investigated the combined effects of type I and type III AFPs on ice recrystallization inhibition (IRI), focusing on whether mixing AFPs with different ice-binding specificities enhances their IRI function. AFP solutions were prepared at total protein concentrations ranging from 5 to 50&#xa0;µg/mL, and the mixing ratios of the two AFPs were systematically varied. Recrystallization rate constants (<i>k</i>) were determined using the Lifshitz–Slyozov–Wagner model. Both AFP types individually reduced <i>k</i> in a concentration-dependent manner; however, no clear synergistic IRI effect was observed in the mixed AFP systems. At low concentrations, the IRI behavior of mixtures corresponded to the concentration-weighted average of the individual AFPs, whereas at higher concentrations the mixtures exhibited antagonistic effects. These findings are consistent with the possibility that the type I and type III AFPs used in this study did not interact cooperatively on the ice surface, likely due to competitive or interfering adsorption. Overall, the findings indicate that effective use of mixed AFP systems may require careful consideration of the binding-surface preferences and spatial adsorption behavior of each AFP.</p>

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Effects of Mixing Type I and Type III Antifreeze Proteins on Ice Recrystallization Inhibition Activity

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年3月12日

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  • Zhaohui Sun,
  • Mario Shibata,
  • Tomoaki Hagiwara

摘要

Ice recrystallization is a major cause of texture and quality deterioration during frozen storage, and antifreeze proteins (AFPs) have attracted attention as potential non-colligative ice-growth inhibitors. This study investigated the combined effects of type I and type III AFPs on ice recrystallization inhibition (IRI), focusing on whether mixing AFPs with different ice-binding specificities enhances their IRI function. AFP solutions were prepared at total protein concentrations ranging from 5 to 50 µg/mL, and the mixing ratios of the two AFPs were systematically varied. Recrystallization rate constants (k) were determined using the Lifshitz–Slyozov–Wagner model. Both AFP types individually reduced k in a concentration-dependent manner; however, no clear synergistic IRI effect was observed in the mixed AFP systems. At low concentrations, the IRI behavior of mixtures corresponded to the concentration-weighted average of the individual AFPs, whereas at higher concentrations the mixtures exhibited antagonistic effects. These findings are consistent with the possibility that the type I and type III AFPs used in this study did not interact cooperatively on the ice surface, likely due to competitive or interfering adsorption. Overall, the findings indicate that effective use of mixed AFP systems may require careful consideration of the binding-surface preferences and spatial adsorption behavior of each AFP.