TY  - JOUR
AU  - LI, Meng
AU  - KANG, Jiaxin
AU  - NING, Xuenan
AU  - WEI, Zikai
AU  - LIAO, Minhe
AU  - JU, Huanhuan
AU  - XIN, Qiuyan
AU  - LIU, Ning
PY  - 2022
TI  - Effect of β-Lactoglobulin on the Thermal Stability of Vitamin E
JO  - Food Science
SN  - 1002-6630
SP  - 42
EP  - 48
VL  - 43
IS  - 6
AB  - 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.
UR  - https://doi.org/10.7506/spkx1002-6630-20201231-358
DO  - 10.7506/spkx1002-6630-20201231-358