Genipin crosslinked sugar beet pectin-whey protein isolate/bovine serum albumin conjugates with enhanced emulsifying properties
Genipin crosslinked sugar beet pectin-whey protein isolate/bovine serum albumin conjugates with enhanced emulsifying properties
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DOI：
10.1016/j.foodhyd.2020.105802
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发表时间：
2020-08-01
影响因子：
10.7
通讯作者：
Yu, Shujuan
中科院分区：
文献类型：
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作者：
Lin, Jiawei;Guo, Xiaoming;Yu, Shujuan
采用京尼平（GP）交联法构建甜菜果胶（SBP）与外源蛋白的偶联物。采用高效分子排阻色谱技术，研究了牛血清白蛋白（BSA）和乳清分离蛋白（WPI）在不同的SBP/外源蛋白质量比（SPR）（2：1-20：1）和交联时间（1-25 h）条件下向SBP分子链的转化过程。当以SPR 10：1制备时，形成的SBP-WPI/BSA-SBP缀合物具有2151的显著更高的分子量。68公斤/摩尔和1758。45 kg/mol，而SBP为289. 16公斤/摩尔）。在反应性方面，WPI在GP与SBP的交联中显示出比BSA更高的反应性。进一步分析交联25小时后以SPR 10：1制备的两种代表性样品SBP-WPI-缀合物和SBP-BSA-缀合物的表面疏水性（S-0）和乳化性质。发现SBP-WPI-缀合物和SBP-BSA-缀合物的S-0值显著低于对照共混物样品的S-0值。此外，与SBP-外源蛋白混合物或单独的SBP和外源蛋白相比，所选择的缀合物显示出上级的乳液稳定特性。在60 ℃下储存7天后，由SBP-WPI-缀合物和SBP-BSA-缀合物稳定的浓度为1g/100 g乳剂的乳剂具有0.735的平均液滴直径。0.023 μ m和0.733 μ m。0.011 μ m，在pH 3.5和0.972。0.020 μ m和1.07. 0.08 pH7.0时，各组分的相对分子质量均为μ m。总之，工作表明GP交联方法适合于将SBP升级为具有增强乳化性质的SBP-蛋白质缀合物。
This work aimed to construct conjugates of sugar beet pectin (SBP) with exogenous proteins by adopting a genipin (GP) crosslinking strategy. The conversion processes of two protein, bovine serum albumin (BSA) and whey protein isolate (WPI) to the molecular chains of SBP were investigated using high-performance sizeexclusion chromatography technology under varying SBP/exogenous protein weight ratios (SPR) (2:1-20:1) and crosslinking times (1-25 h). When prepared at SPR 10:1, the formed SBP-WPI/BSA-SBP conjugates had notably higher molecular weights of 2151. 68 kg/mol and 1758. 45 kg/mol, respectively, in comparison with that of SBP (289. 16 kg/mol). In terms of reactivity, WPI showed higher reactivity than BSA in crosslinking with SBP by GP. Two representative samples, SBP-WPI-Conjugate and SBP-BSA-Conjugate, prepared at SPR 10:1 after 25 h of crosslinking were further analyzed for surface hydrophobicity (S-0) and emulsifying properties. It was found that S-0 values of the SBP-WPI-Conjugate and SBP-BSA-Conjugate were significantly lower than that of the control blend samples. Furthermore, the selected conjugates showed superior emulsion stabilizing properties as compared with SBP-exogenous protein blends or individual SBP and exogenous proteins. After storage at 60 degrees C for 7 d, emulsions stabilized by SBP-WPI-Conjugate and SBP-BSA-Conjugate at concentration of 1 g/100 g emulsion had mean droplet diameters of 0.735. 0.023 mu m and 0.733. 0.011 mu m at pH 3.5, and 0.972. 0.020 mu m and 1.07. 0.08 mu m at pH 7.0, respectively. Altogether, the work demonstrates that the GP crosslinking method is suitable for upgrading SBP to SBP-protein conjugate with enhanced emulsification properties.