食品科学 ›› 2020, Vol. 41 ›› Issue (22): 28-33.doi: 10.7506/spkx1002-6630-20190927-330

• 食品化学 • 上一篇    下一篇

果胶、BSA及壳寡糖相互作用及对BSA负载效果的影响

范丽萍,张立彦,陈列欢   

  1. (1.嘉应学院生命科学学院,广东 梅州 514015;2.华南理工大学食品科学与工程学院,广东 广州 510640;3.仲恺农业工程学院动物科技学院,广东 广州 510225)
  • 出版日期:2020-11-25 发布日期:2020-11-26
  • 基金资助:
    广东省科技计划项目(2014B020204002)

Interactions among Pectin, Chiooligosaccharide, and Bovine Serum Albumin and Their Effects on Loading Efficiency of BSA

FAN Liping, ZHANG Liyan, CHEN Liehuan   

  1. (1. School of Life Science, Jiaying University, Meizhou 514015, China; 2. College of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China; 3. College of Animal Science and Technology, Zhongkai University of Agriculture and Engineering, Guangzhou 510225, China)
  • Online:2020-11-25 Published:2020-11-26

摘要: 通过测定不同复合方式下果胶果胶、牛血清白蛋白(bovine serum albumin,BSA)及壳寡糖(chiooligosaccharide,COS)形成的二元及三元聚电解质复合物(polyelectrolyte complexes,PEC)溶液的浊度、宏观及显微状态、PEC得率及BSA复合率和负载率、PEC超微结构及红外光谱等,探讨三者之间的相互作用及对BSA负载效果的影响。结果表明:复合方式显著影响果胶、COS及BSA所形成的二元及三元PEC的结构、状态及溶液浊度;三者间相互作用以静电结合为主,COS与BSA之间存在竞争,果胶趋向于优先结合COS,形成网状结构PEC,并降低PEC对BSA的结合及负载效果;COS存在时,BSA的二级结构会因果胶构象变化而改变。

关键词: 果胶;牛血清白蛋白;壳寡糖;静电复合;竞争;负载

Abstract: Interactions among pectin, bovine serum albumin (BSA) and chiooligosaccharide (COS), and their effects on the loading efficiency of BSA were investigated through the determination of the turbidity and macroscopic and microscopic properties of binary and ternary polyelectrolyte complex (PEC) solutions of these three compounds, PEC yield, the complexation and loading rate of BSA, and the ultrastructure and Fourier transform infrared (FTIR) spectrum of PEC. The results showed that complexation methods significantly affected the turbidity, structure and state of PEC. The three compounds interacted with each other mainly through electrostatic interactions and COS competed with BSA for interacting with pectin. Pectin preferred to form complexes with a reticular structure with COS, resulting in a lower loading efficiency of PEC for BSA. The secondary structures of BSA changed due to the conformational changes of pectin during complexation in the presence of COS.

Key words: pectin; bovine serum albumin; chitooligosaccharide; electrostatic interaction; competition; loading

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