Characterization of silver carp (Hypophthalmichthys molitrix) myosin protein glycated with konjac oligo-glucomannan
Characterization of silver carp (Hypophthalmichthys molitrix) myosin protein glycated with konjac oligo-glucomannan
复制标题
魔芋低聚葡甘聚糖糖化鲢鱼肌球蛋白的表征
DOI：
10.1016/j.foodhyd.2016.01.019
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发表时间：
2016-06-01
影响因子：
10.7
通讯作者：
Ding, Yuting
中科院分区：
文献类型：
--
作者：
Liu, Jianhua;Xu, Qiuhong;Ding, Yuting
采用可控美拉德反应（MR），用葡甘寡糖（KOG）对鲢鱼肌球蛋白（Ms）进行糖基化。比色计测量和SDS-PAGE分析分别指示MR和糖缀合物形成的发生。通过扫描电子显微镜（SEM）观察到更薄的薄片和非均匀的Ms-KOG缀合物。傅里叶变换红外光谱（FT-IR）表明，酰胺的I，II和III带的MS的糖基化改变。糖基化作用96 h后，等电点由5.3降至3.8。Ms在0.1M NaCl中的溶解度最高，反应12 h时总赖氨酸残基减少了23.6%。当在80 ℃加热60 min时，用KOG糖化24 h的Ms的热稳定性从61.4%有效地提高到95.8%。这些结果表明，用KOG进行MR可以是改善Ms功能特性的有前途的方法。（C）2016 Elsevier Ltd.版权所有。
Silver carp (Hypophthalmichthys molitrix) myosin protein (Ms) was glycated with konjac oligoglucomannan (KOG) by using the controlled Maillard reaction (MR). Colorimeter measurements and SDS-PAGE analysis indicated the occurrence of the MR and glycoconjugates formation, respectively. Thinner sheet and non-homogeneous Ms-KOG conjugates were observed by scanning electron microscope (SEM). Fourier transform infrared spectroscopy (FT-IR) indicated that the amide I, II and III bands of Ms were changed by the glycation. Glycation lowered the isoelectric point from 5.3 to 3.8 when incubated for 96 h. Ms became highly soluble in 0.1 M NaCl with the decrease of 23.6% of the total lysine residues at the reaction time of 12 h. The thermal stability of Ms glycated with KOG for 24 h was effectively improved from 61.4% to 95.8% when heated at 80 degrees C for 60 min. These results suggested that MR with KOG can be a promising way to improve functional properties of Ms. (C) 2016 Elsevier Ltd. All rights reserved.