基于温度分布和水分状态分布的扇贝柱蛋白质加热变性数值模拟  

Numerical Simulation of Protein Denaturation of Scallop Adductors during Heating Based on Temperature Distribution and Water Status Distribution

作　　者：石启龙[1] 刘静 赵亚[1] SHI Qilong;LIU Jing;ZHAO Ya(School of Agricultural Engineering and Food Science,Shandong University of Technology,Zibo 255000,China)

机构地区：[1]山东理工大学农业工程与食品科学学院,山东淄博255000

出　　处：《食品工业科技》2025年第5期239-247,共9页Science and Technology of Food Industry

基　　金：山东省自然科学基金资助项目(ZR2020MC215);江苏省重点研发计划(现代农业)项目(BE2023341)。

摘　　要：蛋白质变性是影响扇贝柱热加工(干燥、真空低温慢煮、高温烹饪等)制品品质的关键点,构建扇贝柱蛋白质变性动力学模型,揭示蛋白质变性及其与水分状态的相关性,对于调控扇贝柱热加工制品品质至关重要。本文采用差示扫描量热仪(differential scanning calorimeter,DSC)获得扇贝柱蛋白质变性动力学参数;基于温度分布与水分状态分布,对扇贝柱蛋白质加热变性进行数值模拟。利用低场核磁共振(low-field nuclear magnetic resonance,LF-NMR)技术探究扇贝柱水分组成及状态分布规律。结果表明,扇贝柱肌球蛋白初始变性温度32.50℃,完全变性温度55.00℃;肌动蛋白初始变性温度51.25℃,完全变性温度77.50℃。超声波(ultrasonic,US)预处理导致肌球蛋白和肌动蛋白变性温度都提高了3.75℃,进而提高了扇贝柱热稳定性。随着蛋白质变性程度增加,强结合水(T_(2b))和弱结合水(T_(21))弛豫时间在小范围内波动(T_(2b) 0.19~0.25 ms,T_(21)1.38~2.97 ms),不易流动水(T_(22))和自由水(T_(23))弛豫时间减少;T_(22)所占比例显著降低,T_(2b)和T_(21)比例略有增加,而T_(23)比例基本保持恒定状态。相比于对照组,US预处理导致T_(22)弛豫时间及其所占比例降低。肌球蛋白和肌动蛋白蛋白变性程度与自由水、不易流动水及其所占比例呈负相关。因此,通过监测扇贝柱水分组成及状态分布,可无损、快速评估扇贝柱肌球蛋白和肌动蛋白加热变性程度。Protein denaturation is the key point affecting quality attributes of the scallop adductors(SA)during thermal processing such as drying,sous-vide cooking and traditional cooking.It is of crucial importance to establish a kinetics model of protein denaturation and reveal its relationship with water status of SA for regulating the quality of SA with thermal processing.Protein denaturation kinetics parameters were obtained by using differential scanning calorimeter(DSC).Protein denaturation during heating was numerically simulated based on the temperature distribution and water status distribution.The water status and distribution was measured by using low-field nuclear magnetic resonance(LFNMR).The result indicated that the initial and complete denaturation temperatures of myosin were 32.50℃and 55.00℃,respectively.While the counterparts of actin were 51.25℃and 77.50℃,respectively.Ultrasonic(US)pre-treatment improved thermal stability of protein because the denaturation temperature of myosin and action was increased by 3.75℃compared to the control group.The relaxation time of the tightly bound water(T_(2b))and loosely bound water(T_(21))fluctuated with a narrow range(T_(2b) 0.19~0.25 ms,T_(21)1.38~2.97 ms),and the immobilized water(T_(22))and free water(T_(23))decreased with the increase of protein denaturation degree.While the proportion of T_(22) decreased significantly,and that of T_(2b) and T_(21) increased slightly,but the proportion of T_(23) remained a dynamic stable state.Compared to the control group,US pretreatment resulted in a decrease in the T_(22) and its proportion.The denaturation of myosin and actin was negatively correlated with the free water,immobilized water and its proportion.Therefore,the denaturation degree of myosin and actin during heating can be non-destructively and quickly evaluated by monitoring the water status and distribution of SA.

关 键 词：扇贝柱 超声波 蛋白质变性 动力学模型 数值模拟 低场核磁共振 

分 类 号：TS254.4[轻工技术与工程—水产品加工及贮藏工程]