Encapsulation of oyster protein hydrolysates in nanoliposomes: Vesicle characteristics, storage stability, in vitro release, and gastrointestinal digestion

In this study, oyster protein hydrolysates (OPH) were obtained from oyster meat by hydrolysis using animal complex proteases and then encapsulated in nanoliposomes. The physicochemical properties, stability, and digestive characteristics of OPH-loaded nanoliposomes were evaluated. The average size and zeta potential ranged from 95.64 to 102.39 nm and from -47.36 to -36.43 mV, respectively. Liposomes containing 4 mg/mL OPH had the highest encapsulation efficiency (74.53%). Fourier transform infrared spectroscopy analysis showed that effective ionic complexation and hydrogen bonding existed between phospholipid and peptides. The liposomes exhibited the highest stability when stored at 4 degrees C. Liposomal encapsulation may protect the antioxidant peptides in OPH during storage and simulated digestion. The nanoliposomes were not hydrolyzed and the structural integrity was maintained in gastric digestion, but exhibited lower stability in the intestinal phase. A prolonged release of OPH from nanoliposomes was also observed as compared with free OPH. Liposome containing protein hydrolysates may be used as a formula in functional foods.

Automated summary

This study evaluated the physicochemical properties, stability, and digestive characteristics of oyster protein hydrolysates (OPH) loaded nanoliposomes. The liposomes showed highest stability when stored at 4 degrees C. Engaging in effective ionic complexation and hydrogen bonding, the liposomal encapsulation protected the antioxidant peptides in OPH during storage and simulated digestion.