食品科学 ›› 0, Vol. ›› Issue (): 0-0.

• 基础研究 •    下一篇

不同地域典型干腌火腿肌原纤维蛋白的氧化特性及体外消化性对比性研究

詹光1,乐怡2,王颖3,孙杨赢4,潘道东3,党亚丽5,何俊6,曹锦轩5   

  1. 1. 宁波大学梅山校区食品与药学学院
    2. 武汉轻工大学
    3. 宁波大学食品科学与工程系
    4. 宁波大学食品与药学学院
    5. 宁波大学
    6. 宁波大学浙江省动物蛋白食品精深加工技术重点实验室
  • 收稿日期:2018-10-05 修回日期:2019-08-28 出版日期:2019-12-15 发布日期:2019-12-24
  • 通讯作者: 曹锦轩 E-mail:caojinxuan@nbu.edu.cn
  • 基金资助:
    国家重点研发计划;国家自然科学基金;浙江省科学基金;现代农业技术体系基金

Study on the Oxidation and in Vitro Digestibility of Myofibrillar Proteins among Different Regions Dry-cured Hams

Guang ZHAN 2, Yali Dang3, 2, 2   

  • Received:2018-10-05 Revised:2019-08-28 Online:2019-12-15 Published:2019-12-24

摘要: 摘要:为比较几种典型干腌火腿的可消化吸收性,本文以巴马火腿、金华火腿、宣威火腿、帕尔玛火腿为原料,研究了4种干腌火腿的肌原纤维蛋白表面疏水性、巯基和二硫键含量、超微结构、蛋白降解程度、消化前后粒径大小及体外消化率。结果表明,金华火腿肌原纤维蛋白的表面疏水性显著高于巴马、宣威、帕尔玛火腿(p<0.05)。微观结构分析显示金华火腿肌原纤维蛋白交联和聚集程度最低,肌原纤维排布更为伸展,帕尔玛火腿聚集程度最大,呈现明显聚集状。SDS-PAGE蛋白谱图显示金华火腿肌原纤维蛋白在体外消化过程中大幅降解,促进了肌原纤维蛋白粒径的降低。体外消化研究表明,经胃蛋白酶和胰蛋白酶及α-凝乳蛋白酶作用后,金华火腿肌原纤维蛋白水解速率最高(p<0.05),帕尔玛火腿肌原纤维蛋白水解速率最低(p<0.05)。这表明疏水基团的暴露和蛋白结构的伸展为消化酶提供了更多的识别位点,促进了金华火腿中肌原纤维蛋白的水解。以上研究表明,肌原纤维蛋白的氧化程度显著影响蛋白的体外消化率。

关键词: 干腌火腿, 肌原纤维蛋白, 表面疏水性, 蛋白结构, 体外消化, 蛋白水解率

Abstract: Abstract: Taking Bama ham, Jinhua ham, Xuanwei ham and Parma ham as the research object to compare the digestibility of several trypical dry-cured hams, some properties of myofibrillar proteins including surface hydrophobicity, sulfhydryl and disulfide bond content, ultrastructure, particle size, and in vitro digestibility were investigated among those dry-cured hams. The results showed that the surface hydrophobicity of myofibrillar proteins of Jinhua ham was significantly higher than that of the others (p<0.05). Ultrastructure analysis of myofibrillar proteins implied that Jinhua ham had the lowest degree of cross-linking or aggregation and the conformation of proteins were more stretched, while Parma ham had the largest degree of aggregation compared with Bama ham and Xuanwei ham. SDS-PAGE revealed that myofibrillar proteins of Jinhua ham significantly degraded during the in vitro digestion, which further promoted the decrease of particle size of myofibrillar proteins. The highest proteolysis rate of myofibrillar proteins was observed in Jinhua ham, while the lowest proteolysis rate was presented in Parma ham after pepsin, trypsin and α-chymotrypsin incubation among four typical dry-cured hams (p<0.05). This study indicated that the exposure of hydrophobic groups and the stretch of proteins could provide more recognition sites for digestive enzymes, which accelerated the hydrolysis of myofibrillar proteins in Jinhua ham. This paper demonstrated that degree of oxidation of myofibrillar protein significantly affected the digestibility of the protein.

Key words: dry-cured ham, myofibrillar proteins, surface hydrophobicity, protein structure, in vitro digestion, proteolysis rate

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