转谷氨酰胺酶诱导的大豆蛋白壳寡糖糖基化和交联修饰对其性质的影响
首发时间:2016-03-22
摘要:本研究利用转谷氨酰胺酶(EC 2.3.2.13)诱导大豆蛋白的壳寡糖糖基化和交联反应,并评估其对大豆蛋白水合、胶体和热学性质的影响。在37℃、pH 7.5下,利用分子质量为5 kDa的壳寡糖和转谷氨酰胺酶,制备出糖基含量为13.6 g/kg蛋白质的糖基化交联大豆蛋白。HPLC和FT-IR分析表明壳寡糖连接于大豆蛋白。与大豆蛋白相比,糖基化交联大豆蛋白的持水性显著提高(从6.32至9.11 g/g蛋白),在分散液中聚集物具有更大的水合半径(从82.9至180.2 nm)和zeta-电位(从?27.7至?31.2 mV)。另外,糖基化交联大豆蛋白的热分解温度由大豆蛋白的290.5℃降低至288.2℃,且质量损失更大,表现出其热稳定性降低。因此,大豆蛋白的壳寡糖糖基化和交联修饰改善其水合和胶体性质,但是降低其热稳定性。
关键词: 大豆蛋白 壳寡糖 转谷氨酰胺酶 糖基化 交联 性质
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Property Changes of the Soy Protein With Transglutaminase-induced Oligochitosan Glycation and Cross-linking
Abstract:Oligochitosan glycation and cross-linking of soy protein induced by transglutaminase (EC 2.3.2.13) and an oligochitosan of 5 kDa were assessed in this study, to reveal the potential impacts on hydration, colloidal, and thermal properties of the product, a glycated and cross-linked soy protein (GC-soy protein). Transglutaminase was used at 37℃ and pH 7.5 to treat soy protein isolate (SPI) in the presence of the oligochatosan, and the GC-soy protein was detected to have glucosamine content of 13.6 g/kg protein. Both HPLC and FI-IR results showed that oligochitosan was conjugated covalently into soy protein. In comparison with SPI, GC-soy protein showed enhanced water-binding capacity (9.11 versus 6.32 g/g protein), could form aggregates with enlarged hydrodynamic radius (180.2 versus 82.9 nm) and much negative zeta-potential (?31.2 versus ?27.7 mV) in the dispersion. GC-soy protein exhibited lower decomposition temperature (288.2oC versus 290.5oC) and greater mass loss upon heating than SPI, indicating lower thermal stability. Oligochitosan glycation and cross-linking of soy protein can improve hydration and colloidal properties, but decrease thermal stability.
Keywords: soy protein oligochitosan transglutaminase glycation cross-linking property
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转谷氨酰胺酶诱导的大豆蛋白壳寡糖糖基化和交联修饰对其性质的影响
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