转谷氨酰胺酶诱导的酪蛋白壳寡糖糖基化和交联修饰对产物界面和流变性质的影响
首发时间:2016-01-21
摘要:本研究分析转谷氨酰胺酶(EC 2.3.2.13)诱导的壳寡糖糖基化和交联反应对酪蛋白界面和流变性质的影响。在37℃、pH为7.5以及分子质量为1 kDa的壳寡糖存在下,利用转谷氨酰胺酶的催化作用对酪蛋白进行糖基化和交联修饰反应,制备糖基化交联酪蛋白。比浊法分析结果表明,与酪蛋白相比,修饰反应导致修饰产物的乳化活性下降14.5%,而乳化稳定性不变。激光共聚焦显微镜扫描分析证实,由修饰产物形成的乳化液有较好的稳定性。搅打法分析结果表明,修饰产物的起泡能力较酪蛋白下降17.3%,但是泡沫稳定性不变。流变分析结果表明,修饰产物分散液的表观黏度显著增加,并且其黏性模量高于弹性模量。因此,所采用壳寡糖糖基化和交联修饰可以有效的改变酪蛋白的功能性质。
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Effects of Oligochitosan Glycation and Cross-linking of Caseinate Induced by Transglutaminase on Its Interfacial and Rheological Properties
Abstract:The oligochitosan glycation and cross-linking of caseinate induced by transglutaminase and an oligochitosan of 1 kDa were assessed for the potential impacts on interfacial and rheological properties of the generated product (glycated and cross-linked caseinte) in this study. Transglutaminase (EC 2.3.2.13) was used to treat the caseinate at 37℃ and pH 7.5 in presence of the oligochatosan. The glycated and cross-linked caseinate exhibited lower emulsifying activity index about 14.5% than caseinate, but its emulsion stability index was statistically the same as that of the caseinate. Confocal laser scanning microscope analysis results confirmed the emulsion formed with the glycated and cross-linked caseinte had good emulsion stability. The glycated and cross-linked caseinte had decreased relative overrun (about 17.3%) and the same foam stability, compared with the caseinate. In addition, the dispersion generated with the glycated and cross-linked caseinate showed the much enhanced apparent viscosity, viscous modulus and elastic modulu than that generated with the caseinate. It is thus concluded that the applied oligochitosan glycation and cross-linking of caseinate is powerful to change the functional properties of caseinate.
Keywords: Caseinate transglutaminase glycation cross-linking functional properties
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转谷氨酰胺酶诱导的酪蛋白壳寡糖糖基化和交联修饰对产物界面和流变性质的影响
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