State Key Laboratory of Marine Food Processing and Safety Control, College of Food Science and Engineering, Ocean University of China, Qingdao 266404, PR China; Qingdao Key Laboratory of Food Biotechnology, Qingdao 266404, PR China; Key Laboratory of Biological Processing of Aquatic Products, China National Light Industry, Qingdao 266404, PR China.
Shandong Meijia Group Co. Ltd., Rizhao 276800, PR China.
Food Chem. 2024 May 30;441:138259. doi: 10.1016/j.foodchem.2023.138259. Epub 2023 Dec 27.
This study aimed to investigate the cryoprotective properties of proline (1% and 3% (w/v)) on shrimp. The cryoprotective mechanism was studied using physico-chemical experiments and molecular simulations. Proline had a notable positive impact on the thawing loss and texture of shrimp in comparison to the control. The denaturation of myosin in frozen shrimp was delayed by proline. Microscopy analysis demonstrated that proline effectively lowered the harm caused by ice crystals to shrimp muscle. Molecular simulations indicated that proline potentially exerted a cryoprotective effect primarily through the "water substitution" and "glassy state" hypotheses. Proline formed hydrogen bonds with myosin to replace the water molecules around myosin. Additionally, proline interacted with water molecules to form a glassy state, impeding the growth of ice crystals. Consequently, the stability of shrimp myosin was enhanced during freezing. In conclusion, proline demonstrated promise as an efficacious cryoprotectant for aquatic products.
本研究旨在探究脯氨酸（1%和 3%（w/v））对虾的抗冻保护特性。通过物理化学实验和分子模拟研究了抗冻保护机制。脯氨酸对虾的解冻损失和质地有显著的积极影响，与对照组相比。脯氨酸延缓了冷冻虾中肌球蛋白的变性。显微镜分析表明，脯氨酸有效地降低了冰晶对虾肌肉的伤害。分子模拟表明，脯氨酸可能主要通过“水替代”和“玻璃态”假说发挥抗冻保护作用。脯氨酸与肌球蛋白形成氢键，取代肌球蛋白周围的水分子。此外，脯氨酸与水分子相互作用形成玻璃态，阻碍冰晶的生长。因此，在冷冻过程中增强了虾肌球蛋白的稳定性。总之，脯氨酸有望成为一种有效的水产品抗冻保护剂。
