Effect of ultrasonic pretreatment on antifreeze activity of gluten antifreeze polypeptide

• Published in: Food science & technology 2024-08, Vol.206, p.116583, Article 116583
• Main Authors: Zhang, Yanyan, Wang, Suo, Xia, Na, Guo, Penglei, li, Yinli, Zhang, Hua, Li, Suyun
• Format: Article
• Language: English
• Subjects: Antifreeze activity; Ice recrystallization inhibition; Thermal hysteresis activity; Ultrasonic pretreatment
• ISSN: 0023-6438
• DOI: 10.1016/j.lwt.2024.116583

In this study, the effects of thermal hysteresis activity, ice recrystallization inhibition, amino acid composition and surface hydrophobicity of different ultrasonic pretreatments on gluten antifreeze polypeptide was studied. The results of the thermal hysteresis activity showed that the collaborative (flat-panel combined probe) ultrasonic working mode was superior to the single-frequence ultrasound mode. In the optimal working mode (15 min, 100 W/L), the results of polarized light microscope and gel chromatography column showed that ultrasonic pretreatment could effectively inhibit the growth of ice crystals, reduced the size of ice crystals, and to a certain extent, transfer the molecular weight distribution of peptides to small molecular peptides. The molecular weight was mainly concentrated at about 200–1000 u. The contents of Valine, Methionine, Leucine, Proline and Glutamic acid residues in the gluten antifreeze polypeptide pretreated by ultrasonic wave were relatively high and more hydrophobic groups were exposed. The secondary structure results showed that the molecular conformation of the polypeptide was mainly α-helix and β-sheet conformations. This paper systematically revealed the intrinsic correlation mechanism between the changes of key domains of substrate proteins and the antifreeze activity of enzymatic hydrolysis products assisted by ultrasoud, providing a theoretical basis for the preparation of antifreeze polypeptide. •Ultrasonic pretreatment improved the thermal hysteresis activity of gluten antifreeze peptides.•Ultrasonic pretreatment exposed more hydrophobic groups of gluten antifreeze peptides.•The molecular conformation of gluten antifreeze polypeptide was mainly α-helix and β-sheet conformations.