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• 食品化学 •    下一篇

没食子酸诱导肌原纤维蛋白巯基和表面疏水性变化对蛋白凝胶特性的影响

贾娜1,林世文2,3,王乐田3,刘登勇3   

  1. 1. 渤海大学食品科学与工程学院
    2.
    3. 渤海大学
  • 收稿日期:2019-08-29 修回日期:2020-08-13 出版日期:2020-11-25 发布日期:2020-11-18
  • 通讯作者: 刘登勇 E-mail:jz_dyliu@126.com
  • 基金资助:
    国家自然科学基金青年项目

Effects of changes in sulfhydryl and surface hydrophobicity of myofibrillar protein induced by gallic acid on gel properties of protein

1, 1,1,Le-Tian WANG   

  • Received:2019-08-29 Revised:2020-08-13 Online:2020-11-25 Published:2020-11-18

摘要: 将没食子酸(0、10、50、100、200 μmol/g)添加到肌原纤维蛋白中,测定蛋白质的巯基含量、表面疏水性、凝胶强度和保水性、流变特性,并对凝胶的微观结构进行观察,研究没食子酸诱导的肌原纤维蛋白巯基和表面疏水性变化对蛋白凝胶特性的影响。结果表明:添加没食子酸使肌原纤维蛋白的巯基含量显著降低(P<0.05),但不同浓度之间差异不显著(P>0.05);没食子酸使表面疏水性显著增加(P<0.05);没食子酸浓度为10 μmol/g时,凝胶强度和保水性与对照相比无显著差异(P>0.05),流变曲线仍与对照相似,当浓度增加至50、100、200 μmol/g时,凝胶强度与保水性显著降低(P<0.05),流变曲线趋于平坦;微观结构显示没食子酸浓度增大,凝胶网络结构逐渐松散,孔隙变大。因此,低浓度的没食子酸对蛋白凝胶特性无不利影响,而高浓度没食子酸可能通过促使蛋白质发生疏水性聚集或生成巯基-醌加成物而削弱蛋白凝胶化程度,降低蛋白凝胶强度与持水能力。

关键词: 没食子酸, 肌原纤维蛋白, 巯基, 表面疏水性, 凝胶特性

Abstract: Gallic acid (0, 10, 50, 100, 200 μmol/g) was added to myofibrillar protein (MP), and the sulfhydryl content, surface hydrophobicity, gel strength, water-holding capacity and rheological properties of the MP were measured. Also, the microstructure of the gel was observed. The effects of changes of sulfhydryl and surface hydrophobicity induced by gallic acid on the gel properties of MP were studied. The results showed that gallic acid significantly reduced the sulfhydryl content (P<0.05), but there was no significant difference among different concentrations (P>0.05). The gallic acid increased the surface hydrophobicity of MP (P<0.05). When the gallic acid concentration was 10 μmol/g, the gel strength and water-holding capacity had no significant difference compared with the control (P>0.05) and the rheological curve was similar to that of the control. When the concentration increased to 50, 100 and 200 μmol/g, the gel strength and water-holding capacity decreased significantly (P<0.05) and the rheological curve was flat. The microstructure showed that when the gallic acid concentration increased, the gel network structure gradually loosened and bigger pores appeared. Therefore, low concentration of gallic acid had no adverse effect on gel properties of MP, while the medium and high concentration of gallic acid impaired protein gelation and reduce protein gel strength and water-holding capacity probably by promoting hydrophobic aggregation or formation of thiol-quinone adducts.

Key words: Gallic acid, Myofibrillar protein, Sulfhydryl group, Surface hydrophobicity, Gel properties

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