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Food Quality and Safety · 2021 · IF 3.102

Low-temperature combined with high-humidity thawing improves the water-holding capacity and biochemical properties of Portunus trituberculatus protein

Ling Jiangang,Xuan Xiaoting,Xu Zihan,Ding Tian,Lin Xudong,Cui Yan,Liu Donghong

This study compared the effects of conventional thawing methods (water immersion thawing (WIT, (25±1) °C), natural air thawing (AT, (25±1) °C, relative humidity (RH) (65±2) per cent), refrigerator thawing (RT, 4 °C, RH (80±2) per cent) and low-temperature (LT) combined with high-humidity thawing (LT, –1 °C to 1 °C (LT–1–1), 2–4 °C (LT2–4), 5–7 °C (LT5–7) and 8–10 °C (LT8–10), RH≥95 per cent) on the water-holding capacity, lipid oxidation and biochemical properties of Portunus trituberculatus (P. trituberculatus) myofibrillar protein. The results showed that WIT and AT significantly decreased the water-holding capacity while dramatically increasing lipid oxidation, protein oxidation and degeneration, resulting in serious P. trituberculatus quality deterioration. High humidity was beneficial for P. trituberculatus thawing. The thawing time of P. trituberculatus under the conditions of LT2–4 was only 39.39 per cent of that of conventional air thawing at 4 °C (RT), and the LT2–4 samples not only maintained better water-holding capacity but also had an obviously reduced degree of lipid oxidation, protein oxidation and denaturation. Thawed samples LT2–4 and LT5–7 provided better maintenance of P. trituberculatus quality than the LT–1–1 and LT8–10 samples. The best quality was exhibited after thawing at 2–4 °C. The levels of thiobarbituric acid reacting substances, carbonyl content and surface hydrophobicity observably decreased in these samples, while the total sulfhydryl contents dramatically increased compared to those of conventionally thawed samples, indicating lower lipid oxidation and protein oxidation. Moreover, the Ca2+-ATPase activity of the sample thawed at 2–4 °C (2.06 μmol Pi/mg prot/h) was markedly higher than that of samples subjected to WIT and AT. The product qualities observed after thawing at –1 °C to 1 °C, 5–7 °C and 8–10 °C under LT were comparable to that observed by RT. Considering its thawing efficiency and product quality, LT is a suitable method for the thawing of P. trituberculatus, and the ideal thawing conditions were LT at 2–4 °C.

研究领域: 食品科学 · 生物化学
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2025 · IF 8.5

Effects of pulsed electric field (PEF) on the gel and protein structural properties of surimi and the underlying mechanisms

Shichen Zhu,Yechun Gong,Canran Bao,Fangdong Yang,Hao Zhu,Shulai Liu,Yuting Ding,Xuxia Zhou

This study systematically investigated the effects of pulsed electric field (PEF) treatments on the gelation properties and protein structural modifications in surimi. Through experimental analyses complemented by molecular dynamics (MD) simulations, we elucidated the molecular mechanisms underlying these changes. Notably, moderate PEF treatment (15 kV/cm, 40 min) significantly enhanced gel strength and water-holding capacity (WHC) by 34.68 % and 11.55 %, respectively, compared to untreated samples. However, excessive parameters (> 20 kV/cm or > 60 min) induced protein over-aggregation through disulfide bond crosslinking, resulting in deteriorated gel quality. MD simulations revealed that PEF-induced alterations in molecular dipole moments accelerated conformational rearrangement of α-helical structures. The synergistic interplay between reinforced hydrogen bonding networks and optimized hydrophobic interactions was identified as the primary determinant of improved gel functionality. These findings collectively highlight the critical balance required in PEF parameter selection for surimi processing optimization.

CAS / MDL: 7647-14-5
研究领域: 食品科学 · 生物物理学
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