Aloe dairy products have occupied a certain market share, and the interaction between the small bioactive molecules contained in aloe and milk proteins during product processing profoundly affects the performance of dairy products. In this study, two typical and potentially dangerous bioactive small molecules of aloe, aloin (AA) and aloe-emodin (AE), were selected to investigate their interaction mechanism with β -lactoglobulin ( β -La). Computer simulations showed that AA/AE had the potential to form complexes with β -La, and the β -La-AA system exhibited a stronger binding affinity than the β -La-AE system. Fluorescence analysis showed that the binding affinity values of AA to β -La at 298 K were deduced to be (4.184 ± 1.06) × 10 4 M −1 , meaning medium-strength interactions, comparatively, AE to β -La was weaker, were deduced to be (3.15 ± 1.25) × 10 3 M −1 . In addition, the thermodynamic analysis found that ΔH 0 and ΔS 0 were positive in both the β -La-AA system and the β -La-AE system, which implies that the main driving force for the combination of AA/AE and β -La to form the ground state complex is the hydrophobic force. The conformation changes in β -La brought about by binding to AA/AE may alter the properties and functions of the protein, such as surface hydrophobicity and oxidation resistance. Analysis shows that β -La is potentially present in whey as an AA/AE carrier during the production of aloe milk.
In terms of the vital functions of barbaloin, it is necessary to develop a selective and sensitive detection means in barbaloin sensing to replace the previous defective analytical methods. Herein, the water-soluble luminescent gold nanoclusters (Au NCs) with good emission character were firstly established for barbaloin detection with high efficiency. The small size and stable probe was synthesized through one-pot way by protecting and reducing of histidine (His). The characterization results revealed that the quenching mechanism was mainly attributed to the inner filter effect (IFE). The His-Au NCs displayed high selectivity to barbaloin against interferes and a good linear relationship existed in the range of 0.5–150 μM. More importantly, the probe was successfully employed to detect barbaloin in bovine serum samples with satisfactory recoveries and the excellent performance was also obtained from temperature sensing. This novel detection platform expanded the analytical methods for barbaloin based on fluorescence properties.