食品科学 ›› 2019, Vol. 40 ›› Issue (19): 89-95.doi: 10.7506/spkx1002-6630-20181011-088

• 基础研究 • 上一篇    下一篇

改性处理对猪肌原纤维蛋白结构及凝胶特性的影响

姜国川,王丽岩,刘亚春,孙洪蕊,张佳霖,刘学军,闫晓慧   

  1. (1.吉林农业大学食品科学与工程学院,吉林 长春 130118;2.吉林省农业科学院农产品加工研究所,吉林 长春 130033;3.吉林省轻工业设计研究院,吉林 长春 130021;4.吉林工商学院财税学院,吉林 长春 130507)
  • 出版日期:2019-10-15 发布日期:2019-10-25
  • 基金资助:
    吉林省科技发展计划项目(20140309015NY)

Effect of Modification on the Structure and Gel Properties of Porcine Myofibrillar Protein

JIANG Guochuan, WANG Liyan, LIU Yachun, SUN Hongrui, ZHANG Jialin, LIU Xuejun, YAN Xiaohui   

  1. (1. College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China; 2. Institute of Agro-food Technology, Jilin Academy of Agricultural Sciences, Changchun 130033, China; 3. Jilin Light Industry Design and Research Institute, Changchun 130021, China; 4. Finance and Taxation College, Jilin Business and Technology College, Changchun 130507, China)
  • Online:2019-10-15 Published:2019-10-25

摘要: 采用超声波改性、谷氨酰胺转氨酶改性、超声波-谷氨酰胺转氨酶复合改性3 种方法对猪肌原纤维蛋白进行改性处理,以凝胶的强度、硬度、弹性、持水性、化学作用力、白度等为评价指标研究改性处理对猪肌原纤维蛋白凝胶特性的影响,以蛋白质二级结构、差示扫描量热、紫外吸收光谱表征改性处理对肌原纤维蛋白结构的影响。结果表明:超声波-谷氨酰胺转氨酶复合改性效果最明显,与对照组相比,其巯基含量降低、持水性增加、白度增加、疏水相互作用力增加,凝胶强度、硬度、弹性分别是对照组的3.57、3.65、1.15 倍。蛋白质结构分析结果表明,超声波-谷氨酰胺转氨酶复合改性后蛋白质热变性温度升高,α-螺旋相对含量下降,β-折叠、β-转角相对含量升高,紫外吸光度增加。改性后蛋白质结构向有利于提高肌原纤维蛋白凝胶特性方向转变。本研究结果为实现肌原纤维蛋白的综合利用提供了理论依据。

关键词: 肌原纤维蛋白, 超声波, 谷氨酰胺转氨酶, 凝胶性, 蛋白结构

Abstract: In order to improve gel properties of porcine myofibrillar protein, we examined the effect of ultrasonic and/or transglutaminase (TG) treatment on gel strength, hardness, elasticity, water-holding capacity and chemical forces of heat-induced myofibrillar protein gels. We also investigated the effect on structural properties of?myofibrillar protein?by protein secondary structure analysis, differential scanning calorimetry and ultraviolet absorption spectroscopy. The results showed that the combined treatment could more significantly modify the properties of myofibrillar protein than either treatment alone. Compared with the control group, the content of sulfhydryl groups decreased, and water-holding capacity, whiteness value and hydrophobic interaction force increased; gel strength, hardness and elasticity values were enhanced by 3.57, 3.65 and 1.15 times in the combined treatment group, respectively. The results of structural analysis indicated that the combined treatment increased the thermal denaturation temperature of myofibrillar protein and resulted in a decrease in the relative content of alpha-helix with a simultaneous an increase in the relative contents of beta-sheet and beta-turn structure. In addition, this treatment increased the ultraviolet absorbance. The modified protein structure was conducive to improving the formation of myofibrillar protein gel. These results provide a theoretical basis for comprehensive utilization of myofibrillar protein.

Key words: myofibrillar protein, ultrasonic, transglutaminase, gel properties, protein structure

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