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β-乳球蛋白对VE热稳定性的影响
引用本文:李萌,康佳欣,宁雪楠,魏子凯,廖敏和,巨欢欢,辛秋艳,刘宁.β-乳球蛋白对VE热稳定性的影响[J].食品科学,2022,43(6):42-48.
作者姓名:李萌  康佳欣  宁雪楠  魏子凯  廖敏和  巨欢欢  辛秋艳  刘宁
作者单位:(1.东北农业大学食品学院,乳品科学教育部重点实验室,黑龙江哈尔滨 150030;2.黑龙江辰鹰乳业有限公司,黑龙江嫩江 161499)
基金项目:“十三五”国家重点研发计划重点专项(2018YFC160430401)
摘    要:为改善超高温瞬时灭菌(ultra-high temperature instantaneous sterilization,UHT)乳中VE的热稳定性,以β-乳球蛋白(β-lactoglobulin,β-LG)和VE为材料制备复合物,探究β-LG对VE热稳定性的影响。通过浊度、粒径、Zeta电位、扫描电子显微镜、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳、红外光谱和荧光光谱研究β-LG与VE的结合情况;利用生物膜干涉技术进一步分析β-LG与VE之间的结合程度;通过高效液相色谱法测定普通强化乳(添加VE)和复合物强化乳(添加β-LG/VE复合物)中UHT前后的VE含量并计算VE热损失率,以确定β-LG对VE热稳定性的影响。结果表明,β-LG可以通过氢键和疏水相互作用与VE结合形成复合物,β-LG与VE结合后,可以减少VE在水溶液中的聚集,使VE的溶解性增加;生物膜干涉技术也证明β-LG与VE之间存在结合,亲和力常数为7.493×10-2?mol/L;复合物强化乳中VE损失率为(4.01±0.18)%,显著低于普通强化乳((10.90±0.17)%)(P<0.05)。以上说明,β-LG可以显著提高VE的热稳定性,为开发维生素强化乳制品提供理论基础。

关 键 词:β-乳球蛋白  VE  生物膜干涉技术  超高温瞬时灭菌乳  热稳定性  

Effect of β-Lactoglobulin on the Thermal Stability of Vitamin E
LI Meng,KANG Jiaxin,NING Xuenan,WEI Zikai,LIAO Minhe,JU Huanhuan,XIN Qiuyan,LIU Ning.Effect of β-Lactoglobulin on the Thermal Stability of Vitamin E[J].Food Science,2022,43(6):42-48.
Authors:LI Meng  KANG Jiaxin  NING Xuenan  WEI Zikai  LIAO Minhe  JU Huanhuan  XIN Qiuyan  LIU Ning
Affiliation:(1. Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, China; 2. Heilongjiang Chenying Dairy Co. Ltd., Nenjiang 161499, China)
Abstract:In order to improve the thermal stability of vitamin E (VE) in ultra-high temperature sterilized (UHT) milk, a complex of β-lactoglobulin (β-LG) with VE was prepared. Turbidity, particle size, zeta potential, scanning electron microscopy, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), infrared spectroscopy and fluorescence spectroscopy were used to explore whether β-LG combined with VE. The degree of binding was further analyzed by bio-layer interferometry. The contents of VE in common fortified milk (with VE) and complex fortified milk (with β-LG/VE complex) before and after ultra-high temperature sterilization were determined by high performance liquid chromatography (HPLC) and the loss rate of VE was calculated to determine the effect of β-LG on the thermal stability of VE. The results showed that β-LG combined with VE to form a complex through hydrogen bonds and hydrophobic interaction, and that binding to β-LG reduced the aggregation of VE in aqueous solution and increased its solubility. Bio-layer interferometry corroborated the binding between β-LG and VE, and the binding constant was 7.493 × 10-2 mol/L. The loss rate of VE in complex fortified milk was significantly lower than that in common fortified milk, (4.01 ± 0.18)% versus (10.90 ± 0.17)% (P < 0.05). The above results showed that β-LG/VE could effectively improve the thermal stability of VE, which provides a theoretical basis for the development of vitamin fortified dairy products.
Keywords:β-lactoglobulin  vitamin E  bio-layer interferometry  ultra-high temperature sterilized milk  thermal stability  
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