研究报告

葡聚糖分子质量对其与牛血清白蛋白共聚物性质的影响

  • 张晓燕 ,
  • 孟令莉 ,
  • 吴子健 ,
  • 刘丹丹 ,
  • 赵颖涛
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  • 1(天津商业大学 生物技术与食品科学学院,天津市食品生物技术重点实验室,天津,300134)
    2(天津商业大学 艺术学院,天津,300134)
硕士研究生(吴子健教授为通讯作者,E-mail:wzjian@tjcu.edu.cn)

收稿日期: 2020-11-23

  修回日期: 2021-01-20

  网络出版日期: 2021-08-23

基金资助

天津市应用基础与前沿技术研究计划项目(19JCTPJC54600);天津市重点研发计划项目(19YFLHSN00080)

Effects of dextran molecular weight on characteristics of BSA-dextran conjugates

  • ZHANG Xiaoyan ,
  • MENG Lingli ,
  • WU Zijian ,
  • LIU Dandan ,
  • ZHAO Yingtao
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  • 1(School of Biotechnology and Food Science,Tianjin University of Commerce,Tianjin Key Laboratory of Food Biotechnology,Tianjin 300134,China)
    2(School of Art,Tianjin University of Commerce,Tianjin 300134,China)

Received date: 2020-11-23

  Revised date: 2021-01-20

  Online published: 2021-08-23

摘要

采用干热接枝法制备牛血清白蛋白(bovine serum albumin,BSA)与不同分子质量(1 k、5 k、70 k和100 kDa)葡聚糖的共聚物(BSA-dextran conjugate,BDC),探讨葡聚糖分子质量对BSA的结构及其乳浊液流变性质的影响。BDC的SDS-PAGE电泳图谱、红外光谱分析及接枝度结果证明了干热接枝反应的发生,且葡聚糖的分子质量影响接枝度的大小。共聚物的三级结构中,BDC 5变得更加松散,结构的变化引起分子间的疏水作用降低,表面疏水性达到(6.876±0.69),且乳化性达到(49.06±0.85)m2/g;而BDC 100的乳化稳定性最高为(57.357±1.02),葡聚糖的接枝还能改善BSA的起泡性和泡沫稳定性;乳浊液的流变特性表明,随着葡聚糖的分子质量增加,BDC的黏度会增大,其中BDC 100的黏度最大。研究结果可为改善BSA的功能性和深入了解BSA的改性机制提供理论依据。

本文引用格式

张晓燕 , 孟令莉 , 吴子健 , 刘丹丹 , 赵颖涛 . 葡聚糖分子质量对其与牛血清白蛋白共聚物性质的影响[J]. 食品与发酵工业, 2021 , 47(15) : 104 -110 . DOI: 10.13995/j.cnki.11-1802/ts.026173

Abstract

BSA-dextran conjugates (BDC), which was composed of bovine serum albumin (BSA) and dextran (DEX) with different molecular weights (1 k, 5 k, 70 k and 100 kDa), was prepared by dry heating grafting method. And then, the influence of dextran molecular weight on the structure of BSA and also the rheological properties of BDC emulsion was explored. Results of SDS-PAGE electrophoresis, infrared spectrum analysis and BDC graft degree proved that the dry-heat grafting reaction had occurred, and the molecular weight of dextran affected the grafting degree. In the tertiary structure of the copolymer, BDC 5 becomes looser, and the change of the structure caused the hydrophobic interaction between molecules to decrease. The surface hydrophobicity reached (6.876±0.69), and the emulsifying activity index reached (49.06±0.85) m2/g; BDC 100 possessed the highest emulsification stability(57.357±1.02). Grafting of dextran to BSA could improve the foaming and foam stability of BSA; the rheological properties of the emulsion indicated that,with the molecular weight of dextran increased, the viscosity of BDC also increased and BDC 100 having the largest viscosity. This research results provide a theoretical basis for improving the functionality of bovine serum albumin and understanding the modification mechanism of bovine serum albumin.

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