Effects of pulsed electric fields processing on stability of egg white proteins
Effects of pulsed electric fields processing on stability of egg white proteins
复制标题
脉冲电场处理对蛋清蛋白稳定性的影响
DOI：
10.1016/j.jfoodeng.2014.04.008
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发表时间：
2014-10-01
影响因子：
5.5
通讯作者：
Chen, Xiaochan
中科院分区：
文献类型：
--
作者：
Wu, Li;Zhao, Wei;Chen, Xiaochan
采用胶体性质、蛋白质氧化和电泳谱等方法研究了蛋清溶液在脉冲电场(PEP)处理过程中的变化。在25千伏/厘米的电场强度下处理400亩S没有改变蛋白质溶液的胶体性质，包括可溶性蛋白质含量、Z-平均尺寸、多分散指数和Zeta电位。但当处理时间超过600m时，S出现一个大颗粒的小峰，可溶性蛋白质含量(7.84%)下降，Z-平均颗粒增大(36.9%)。在PEF处理过程中，游离巯基含量略有增加，蛋白质羰基含量没有增加。这反映了蛋白质在所有处理过程中并没有发生氧化，但部分蛋白质解折叠或SH电离增强。电泳图显示了异质蛋白之间的共价和非共价结合所产生的不可溶聚集体。不溶性聚集体的主要成分是溶菌酶、卵清蛋白和卵转铁蛋白。(C)2014爱思唯尔有限公司。保留所有权利。
Colloidal properties, protein oxidation and electrophoresis patterns were used to investigate the changes of egg white solution during Pulsed Electric Field (PEP) processing. Treatment at electric field strength of 25 kV/cm for 400 mu s did not change the protein solution colloidal properties, including soluble protein content, Z-average size, PDI (polydispersity index) and zeta potential. However, when the processing time exceeded 600 mu s, accompany with a small peak of large particle size appeared, a decrease in soluble protein content (7.84%) and an increase in Z-average size (36.9%) was observed. A slight increase in free sulfhydryl content and no increase in protein carbonyl content detected during PEF treatments. This reflected that protein oxidation did not occur during all treatments but partial protein unfolding or SH ionization was enhanced. Electrophoresis patterns showed insoluble aggregates resulting from covalent and non-covalent binding between heterogeneous proteins. The main components of the insoluble aggregates were lysozyme, ovalbumin and ovotransferrin. (C) 2014 Elsevier Ltd. All rights reserved.