食品科学 ›› 2019, Vol. 40 ›› Issue (4): 186-191.doi: 10.7506/spkx1002-6630-20180122-289

• 生物工程 • 上一篇    下一篇

棒状乳杆菌发酵秘鲁鱿鱼糜凝胶特性的变化及其形成机理

陈晓倩,吴祖芳*,翁佩芳   

  1. (宁波大学海洋学院,应用海洋生物技术教育部重点实验室,浙江 宁波 315211)
  • 出版日期:2019-02-25 发布日期:2019-03-05
  • 基金资助:
    宁波市科技富民项目(2016C10031)

Changes in Gel Properties and Formation Mechanism of Giant Squid Surimi (Dosidicus gigas) during Fermentation by Lactobacillus coryneformis

CHEN Xiaoqian, WU Zufang*, WENG Peifang   

  1. (Key Laboratory of Applied Marine Biotechnology, Ministry of Education, School of Marine Science, Ningbo University, Ningbo 315211, China)
  • Online:2019-02-25 Published:2019-03-05

摘要: 为阐明棒状乳杆菌(Lactobacillus coryniformis)Lz153发酵秘鲁鱿鱼糜的凝胶形成机理,通过质构仪测定棒状乳杆菌Lz153发酵秘鲁鱿鱼糜凝胶特性,分析凝胶形成过程中离子键、氢键、疏水相互作用、二硫键及非二硫共价键的变化,并利用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)方法观察肌原纤维蛋白变化情况。结果表明,棒状乳杆菌Lz153鱿鱼糜发酵24~36?h阶段凝胶特性最佳;离子键含量在发酵过程中呈逐渐减少趋势,氢键和疏水相互作用含量分别在发酵36?h和30?h达到最大值,二硫键和非二硫共价键含量随发酵时间延长而呈增加的趋势;氢键、疏水相互作用、二硫键和非二硫共价键是形成和维持凝胶网络的主要作用力。SDS-PAGE图谱显示,发酵后肌动蛋白和肌球蛋白重链均开始被降解,同时经发酵24?h后分子质量在100~135?kDa范围出现了新的盐溶性蛋白质条带,发酵至48?h也被降解。研究结果可为开发秘鲁鱿鱼为原料的乳酸菌发酵鱼糜制品加工提供参考依据。

关键词: 秘鲁鱿鱼鱼糜, 棒状乳杆菌Lz153, 凝胶形成, 化学作用力, 肌原纤维蛋白

Abstract: The gel properties of giant squid surimi (Dosidicus gigas) fermented by Lactobacillus coryniformis Lz153 were determined by a texture analyzer. Changes in chemical forces including ionic bond, hydrogen bond, hydrophobic interaction, disulfide bond and non-disulfide covalent bond were examined during the gel formation process, and changes in myofibrillar protein were monitored by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The aim of this study was to determine the mechanism of gel formation. The results showed that the best gel characteristics were achieved between 24 and 36 h of fermentation. Ionic bond content decreased gradually during the fermentation process, and the contents of hydrogen bond and hydrophobic force reached the maximum values at 36 and 30 h, respectively. The contents of disulfide bond and non-disulfide covalent bond increased with the prolongation of fermentation time. Hydrogen bond, hydrophobic force, disulfide bond and non-disulfide covalent bond were the main driving forces for gel formation. SDS-PAGE showed that the myosin heavy chain and actin were degraded gradually during fermentation. Meanwhile, a new salt-soluble protein band within the range of 100–135 kDa appeared at 24 h and was gradually degraded till 48 h. Our results provide a basis for the production of lactic acid bacteria fermented surimi from giant squid muscle.

Key words: giant squid surimi, Lactobacillus coryniformis, gel formation, chemical forces, myofibrillar proteins

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