| 鸢乌贼酶解产物的抗氧化稳定性与功能特性 |
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| 引用本文： | 荣婧, 仇超颖, 胡晓, 杨贤庆, 李来好. 鸢乌贼肌原纤维蛋白糖基化产物功能特性研究[J]. 南方水产科学, 2018, 14(1): 68-76. DOI: 10.3969/j.issn.2095-0780.2018.01.009 |
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| 作者姓名： | 荣婧 仇超颖 胡晓 杨贤庆 李来好 |
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| 作者单位： | 1.中国海洋大学食品科学与工程学院，山东 青岛 266003;2.中国水产科学研究院南海水产研究所，农业部水产品加工重点实验室，国家水产品加工技术研发中心，广东 广州 510300 |
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| 基金项目： | 中国水产科学研究院中央级公益性科研院所基本科研业务费专项资金资助 (2016PT09)；农业部水产品加工重点实验室开放基金 (NYJG201511)；中国水产科学研究院南海水产研究所中央级公益性科研院所基本科研业务费专项资金资助 (2015TS29)；国家自然科学基金青年基金项目(31601503) |
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| 摘 要： | 以葡聚糖、褐藻寡糖、葡萄糖、乳糖为糖基供体实现对鸢乌贼(Symplectoteuthis oualaniensis)肌原纤维蛋白糖基化改性，分析了不同糖的种类及改性时间对蛋白溶解性、结构、乳化性、起泡性等功能性质的影响。结果表明，肌原纤维蛋白与不同种类的糖质量比1∶1反应12 h后，SDS-PAGE分析显示糖基化产物分子量明显增大，小分子糖与肌原纤维蛋白反应更快；糖基化反应使肌原纤维蛋白的溶解性显著提高，表面疏水性降低；此外，肌原纤维蛋白二级结构明显改变，β-转角含量显著升高，β-折叠含量降低。糖基化反应未能改善肌原纤维蛋白的热稳定性。反应后的肌原纤维蛋白具有更好的起泡性及起泡稳定性，但乳化性和乳化稳定性降低。肌原纤维蛋白糖基化后在高离子浓度氯化钠(NaCl)溶液中比在低离子浓度溶液中具有更高的乳化和起泡能力。同时，经糖基化改性的蛋白在低离子浓度时的溶解性和起泡能力也能得到明显改善。
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| 关 键 词： | 鸢乌贼 肌原纤维蛋白 糖基化 乳化性 起泡能力 |
| 收稿时间： | 2017-06-07 |
| 修稿时间： | 2017-08-21 |
Chemical properties and antioxidative activity of glycated alpha-lactalbumin with a rare sugar,D-allose,by Maillard reaction |
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| RONG Jing, QIU Chaoying, HU Xiao, YANG Xianqing, LI Laihao. Functional properties of glycosylated myofibrillar proteins from purple back flying squids (Symplectoteuthis oualaniensis)[J]. South China Fisheries Science, 2018, 14(1): 68-76. DOI: 10.3969/j.issn.2095-0780.2018.01.009 |
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| Authors: | RONG Jing QIU Chaoying HU Xiao YANG Xianqing LI Laihao |
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| Affiliation: | 1.College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China;2.Key Laboratory of Aquatic Product Processing, Ministry of Agriculture; National R&D Center for Aquatic Product Processing; South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China |
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| Abstract: | The myofibrillar proteins extracted from purple back flying squids (Symplectoteuthis oualaniensis) were glycosylated with dextran, alginate oligosaccharide, glucose and lactose. The protein solubility, structure, emulsifying and foaming properties were evaluated. The results show that after saccharides mixing with myofibrillar by 1∶1 (w/w) for 12 h, the SDS-PAGE bands of protein exhibited greater molecular weight, and low molecular saccharides reacted with myofibrillar proteins faster. The protein solubility was improved but the surface hydrophobicity decreased. The secondary structure showed higher β-turn but lower β-sheets content after reaction. Glycosylation did not improve thermal stability of protein effectively. The foaming property and foam stability of glycosylated products were improved while the emulsifying ability and emusion stability decreased. The emulsifying and foaming ability and stability were better in higher ionic solution than in lower ionic solution. The solubility and foaming ability of protein in low ionic solution can be improved effectively, which is meaningful for the application of myofibrillar protein from squids. |
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| Keywords: | squids myofibrillar proteins glycosylation emulsifying properties foaming ability |
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