食品科学 ›› 2023, Vol. 44 ›› Issue (23): 13-20.doi: 10.7506/spkx1002-6630-20230625-183

• 食品非热加工专栏 • 上一篇    下一篇

高强度超声处理时间对克氏原螯虾肌原纤维蛋白理化性质的影响

王子凌, 熊可心, 蒋景淳, 王海滨, 路洪艳, 彭利娟, 廖鄂, 邹圣碧   

  1. (1.武汉轻工大学食品科学与工程学院,湖北 武汉 430023;2.农产品加工与转化湖北省重点实验室,湖北 武汉 430023;3.国家小龙虾加工技术研发分中心(潜江),湖北 潜江 433100)
  • 出版日期:2023-12-15 发布日期:2024-01-02
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2019YFC1606005)

Effect of High-Intensity Ultrasonic Treatment Time on Physicochemical Properties of Myofibrillar Protein from Procambarus clarkii

WANG Ziling, XIONG Kexin, JIANG Jingchun, WANG Haibin, LU Hongyan, PENG Lijuan, LIAO E, ZOU Shengbi   

  1. (1. College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China;2. Hubei Key Laboratory for Processing and Transformation of Agricultural Products, Wuhan 430023, China;3. National R & D Branch Center for Crawfish Processing Technology (Qianjiang), Qianjiang 433100, China)
  • Online:2023-12-15 Published:2024-01-02

摘要: 近年来,超声波作为一种非热、绿色加工技术已被广泛应用于食品行业,但超声处理对克氏原螯虾(又称小龙虾,Procambarus clarkii)肌原纤维蛋白理化性质的具体影响尚不明确。为探究高强度超声对小龙虾肌原纤维蛋白的影响,本实验采用300 W的超声功率、20 kHz的超声频率对小龙虾肉肌原纤维蛋白溶液匀浆分别处理0、4、8、12、16 min,通过测定相关指标分析高强度超声处理对肌原纤维蛋白结构的影响。结果表明,高强度超声波会使小龙虾肌原纤维蛋白浊度和平均粒径显著减小(P<0.05),而溶解度、ζ电位绝对值先上升后下降,表明超声处理会使蛋白聚集程度发生改变;随着处理时间的延长,小龙虾肌原纤维蛋白表面疏水性和内源荧光强度呈现先上升后下降的趋势,总巯基含量显著下降(P<0.05),羰基含量显著上升(P<0.05),表明其三级结构发生了改变,并且发生一定程度的变性;α-螺旋、无规卷曲相对含量先增加后减少,β-转角相对含量先显著增加后显著减少,β-折叠相对含量先显著减少后显著增加,表明其二级结构发生了改变。综上所述,高强度超声处理对小龙虾肉肌原纤维蛋白的理化性质、结构和聚集程度均会产生影响,此结论可为小龙虾加工与贮藏过程中辅助使用超声波技术提供一定的参考。

关键词: 克氏原螯虾;肌原纤维蛋白;结构;聚集程度;高强度超声

Abstract: In recent years, ultrasound has been widely used in the food industry as a promising non-thermal, green technology, but the exact effect of ultrasound on the physicochemical properties of myofibrillar proteins from Procambarus clarkii is not clear yet. This study investigated the effect of high-intensity ultrasound treatment at 300 W power and 20 kHz frequency for 0, 4, 8, 12 and 16 min during homogenization on the structure and physicochemical properties of myofibrillar proteins from Procambarus clarkii. The results showed that ultrasound treatment decreased the turbidity and mean particle size of myofibrillar proteins significantly (P < 0.05), but initially increased and then decreased the solubility and absolute value of ζ-potential, demonstrating altered degree of protein aggregation. The surface hydrophobicity and endogenous fluorescence intensity initially increased and then decreased with increasing treatment time; the total sulfhydryl group content significantly decreased (P < 0.05) while the carbonyl group content significantly increased (P < 0.05), demonstrating changes in the tertiary structure and a certain degree of protein denaturation. In addition, the relative contents of α-helix and random coil increased first and then decreased, whereas the opposite trend was observed for the proportion of β-sheet, indicating changes in the secondary structure. These results showed that high-intensity ultrasound treatment could affect the physicochemical properties, structure and aggregation degree of myofibrillar proteins from crayfish meat, which could provide a reference for the application of ultrasound as an auxiliary approach in the processing and storage of crayfish.

Key words: Procambarus clarkii; myofibrillar proteins; structure; degree of aggregation; high-intensity ultrasound

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