小虾
脯氨酸
肌球蛋白
低温保护剂
变性(裂变材料)
立陶宛
生物化学
凝结
化学
生物物理学
生物
食品科学
氨基酸
渔业
低温保存
核化学
胚胎
物理
热力学
作者
Yejun Zhang,Zhaohui Chen,Yongzhen Wang,Hui Dong,Jianan Sun,Jiao Li,Xiangzhao Mao
标识
DOI:10.1016/j.foodchem.2023.138259
摘要
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.
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