食品科学与技术

大豆可溶性多糖对大豆分离蛋白的物性修饰

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  • 华南理工大学 食品科学与工程学院,广东 广州 510640
齐军茹( 1977-) ,女,博士,教授,主要从事植物蛋白物性修饰研究.

收稿日期: 2016-06-12

  修回日期: 2017-05-03

  网络出版日期: 2017-08-30

基金资助

国家自然科学基金资助项目( 31370036 ) ; 华南理工大学中央高校基本科研业务费专项资金资助项目( 2015Z2119)

Modification of Physicochemical Properties of Soy Protein Isolate by Soybean Soluble Polysaccharide

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  • School of Food Science and Engineering,South China University of Technology,Guangzhou 510640,Guangdong,China
齐军茹( 1977-) ,女,博士,教授,主要从事植物蛋白物性修饰研究.

Received date: 2016-06-12

  Revised date: 2017-05-03

  Online published: 2017-08-30

Supported by

Supported by the National Natural Science Foundation of China( 31370036)

摘要

在60℃,相对湿度为79%的条件下,通过Maillard 反应进行共价接枝,得到大豆分离蛋白( SPI) - 大豆可溶性多糖( SSPS) 共价接枝物( SSC) . 根据糖基化产物在SPI 等电点附近( pH = 4. 5) 和中性条件( pH = 6. 5) 下的溶解性将其分成两个组分SC45 和SC65,对其进行SDS-PAGE 凝胶电泳,并分析了其浊度、粒径和Zeta 电位等物化性质. 结果显示: 反应后生成大相对分子质量的接枝物,SPI 的7S 和11S 中各亚基均参与了糖基化反应,SSC 两个组分的接枝度分别高达41. 79%和36. 75%; SC45 在酸性环境中的浊度显著低于SC65,说明SC45 在蛋白的等电点附近溶解性能优越,能有效降低蛋白的自聚集;SSC 的稳定性主要是由接入的SSPS 分子亲水侧链空间位阻作用提供的.

本文引用格式

齐军茹 曹静 程萌 张曦 杨晓泉 . 大豆可溶性多糖对大豆分离蛋白的物性修饰[J]. 华南理工大学学报(自然科学版), 2017 , 45(9) : 60 -66 . DOI: 10.3969/j.issn.1000-565X.2017.09.009

Abstract

Soy protein isolate ( SPI ) -soybean soluble polysaccharide ( SSPS) conjugates ( SSC) were prepared through a Maillard reaction at 60℃ for seven days with a relative humidity of 79%.Then,the product was separated into two components ( namely,SC45 and SC65) on the basis of their solubility at pH4. 5 ( near the isoelectric point of the SPI) and pH6. 5 ( neutral condition) respectively.Finally,the two components were characterized through SDS-PAGE and were analyzed in terms of turbidity,particle size and Zeta potential.The results show that ( 1) the graft of a higher relative molecular mass forms after the reaction,and each subunit in the 7S and 11S of the SPI is involved in the glycation reaction; ( 2) the graft degrees of the two components are respectively up to 41. 79% and 36. 75%; ( 3) in acid conditions,the turbidity of SC45 is significantly lower than that of SC65,meaning that SC45 has a better solubility near the isoelectric point and can effectively reduce the self-aggregation of the protein; and ( 4) the stability of the SSC depends on the steric hindrance caused by the hydrophilic side chains of the SSPS.
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