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中国精品科技期刊2020
梁雯雯, 郭建, 汪秋宽, 武龙, 任丹丹, 何云海, 陈胜军, 丛海花. 不同解冻方式对鲢鱼肌球蛋白结构和性质的影响[J]. 食品工业科技, 2019, 40(21): 7-12. DOI: 10.13386/j.issn1002-0306.2019.21.002
引用本文: 梁雯雯, 郭建, 汪秋宽, 武龙, 任丹丹, 何云海, 陈胜军, 丛海花. 不同解冻方式对鲢鱼肌球蛋白结构和性质的影响[J]. 食品工业科技, 2019, 40(21): 7-12. DOI: 10.13386/j.issn1002-0306.2019.21.002
LIANG Wen-wen, GUO Jian, WANG Qiu-kuan, WU Long, REN Dan-dan, HE Yun-hai, CHEN Sheng-jun, CONG Hai-hua. Effects of Different Thawing Methods on the Structure and Properties of Silver Carp Myosin[J]. Science and Technology of Food Industry, 2019, 40(21): 7-12. DOI: 10.13386/j.issn1002-0306.2019.21.002
Citation: LIANG Wen-wen, GUO Jian, WANG Qiu-kuan, WU Long, REN Dan-dan, HE Yun-hai, CHEN Sheng-jun, CONG Hai-hua. Effects of Different Thawing Methods on the Structure and Properties of Silver Carp Myosin[J]. Science and Technology of Food Industry, 2019, 40(21): 7-12. DOI: 10.13386/j.issn1002-0306.2019.21.002

不同解冻方式对鲢鱼肌球蛋白结构和性质的影响

Effects of Different Thawing Methods on the Structure and Properties of Silver Carp Myosin

  • 摘要: 为探究不同解冻方式对鲢鱼(Hypophthalmichehys molitrix)肌球蛋白结构和性质的影响,选取冷水解冻、微波解冻、微波-冷水联合解冻三种方式进行解冻处理,通过测定巯基含量、表面疏水性、溶解度、色氨酸荧光光谱、傅里叶红外转换光谱及热稳定性,综合比较解冻后鲢鱼肌球蛋白的结构和性质。结果表明:三种解冻方式之间巯基含量、溶解度无显著差异(P>0.05),微波解冻后肌球蛋白巯基含量较高,为23.74 nmol/mg,冷水解冻后溶解度含量较高,为79.68%;微波解冻和冷水解冻表面疏水性差异显著(P<0.05);傅里叶红外转换光谱显示微波解冻后肌球蛋白变性程度最低;不同解冻方式对肌球蛋白的荧光光谱形状影响不明显,但对荧光强度影响较大,冷水解冻方式下肌球蛋白三级结构展开严重,肌球蛋白热稳定性最差。总体结果表明,微波解冻对鲢鱼肌球蛋白的结构和性质影响相对较小,需进一步从分子层面研究解冻方式对鲢鱼肌球蛋白的影响机制。

     

    Abstract: In order to investigate the effects of different thawing methods on the structure and properties of myosin in Hypophthalmichehys molitrix,three thawing methods,namely cold water thawing,microwave thawing and microwave-cold water combined thawing,were used to thaw the myosin. The sulfhydryl content,surface hydrophobicity,solubility,tryptophan fluorescence spectrum,Fourier transform infrared spectroscopy and thermal stability were determined. The structure and properties of myosin of silver carp after thawing were compared comprehensively. There was no significant difference in sulfhydryl content and solubility among three thawing methods(P>0.05). The sulfhydryl content in myosin after microwave thawing was 23.74 nmol/mg,and the solubility after cold water thawing was 79.68%.There were significant differences in surface hydrophobicity between microwave thawing and cold water thawing(P<0.05). Fourier transform infrared spectrum showed that the degree of myosin degeneration was the lowest after microwave thawing. Different thawing modes had no obvious influence on the shape of myosin fluorescence spectrum,but cold water thawing had an influence on the fluorescence intensity. The tertiary structure of myosin was seriously expanded under cold water thawing,and the thermal stability of myosin was worst. The results showed that microwave thawing had little effect on the structure and properties of silver carp myosin,the effect of thawing method on silver carp myosin should be studied on molecular level.

     

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