The combined effects of succinic anhydride (SA) succinylation and linear dextrin (LD) glycation on whey protein hydrolysates (WPH) and their stabilized emulsions were evaluated. Degree of succinylation (DS), degree of glycation (DG), and degree of browning of samples suggested that a competitive displacement of reactive groups existed when WPH reacted with SA and LD in different orders. Attenuated total reflection Fourier transform infrared (ATR-FTIR) and far-UV circular dichroism (CD) indicated that the order of modification methods had a significant effect on secondary structures of WPH. Succinylation combined with glycation effectively reduced the surface hydrophobicity and increased the molecular flexibility of WPH. Meanwhile, the total free −SH content decreased, and the exposed free −SH content increased. Results of storage stability and gastrointestinal fate of the curcumin-loaded emulsion revealed that the modified WPH with higher DS was more effective for improving the curcumin bioaccessibility, while that with higher DG was more effective for enhancing the stability of the emulsion.
In this study, the influence of pH on the conformational state of EHT, which was obtained from the enzymatic hydrolysis of trypsin, and the stabilizing properties of high internal phase emulsions have been demonstrated. Critical micelle concentration and transmission electron microscopy results exhibited the formation of micellar nanoparticles with mean diameters ranging from 108 to 1359.5 nm. The results of solubility, surface hydrophobicity, and conformations indicated that EHT tended to act as particulate emulsifiers at pH 3, 5, and 7, while at alkaline pH, it was more like a polymeric emulsifier, which could be proven by confocal laser scanning microscopy. The EHT at pH 7 exhibited better stabilizing properties than those at pH 9 and 11 as influenced by storage, temperature, and ionic strength. These findings might be of great importance for broadening the range of sustainable applications of amphiphilic peptides in foods and pharmaceuticals.
Pea protein isolate nanoparticles (PPINs) were successfully prepared by potassium metabisulfite (K 2 S 2 O 5 ). The disulfide bonds were disrupted by K 2 S 2 O 5 , and then the PPINs were formed through self-assembly. The average diameter of PPINs increased from 124.7 to 297.5 nm as the concentration of K 2 S 2 O 5 was increased from 2 to 8 mM, and the PPINs showed higher ζpotentials (−32.2 to −35.8 mV) and unimodal distribution. The content of free sulfhydryl groups first increased and then decreased with the fracture and reformation of disulfide bonds. Subsequently, the increase of the β-sheet, which has considerable hydrophobicity, promoted the formation of PPINs. The formation mechanism of PPINs was explored by dissociation tests: hydrophobic interactions maintained the basic skeleton of PPINs, disulfide bonds stabilized the internal structure, and hydrogen bonds existed on the exterior of the particles. This study provided a simple and economical method to fabricate nanoparticles.
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