In VitroCalcium-Chelating and Platelet Anti-Aggregation Activities of Soy Protein Hydrolysate Modified by the Alcalase-Catalyzed Plastein Reaction

Abstract

Soy protein hydrolysate (SPH) (1 mg/mL), generated by alcalase, had a calcium‐chelating activity of 41 mg/g peptide. The alcalase‐catalyzed plastein reaction of SPH was carried out in different media: ethanol–water, methanol–water and water. The effects of SPH and of resulting modified hydrolysates on calcium‐chelating activities and inhibition of calcium precipitation and platelet aggregation were assessed in vitro. The optimum ethanol concentration, alcalase level and reaction temperature for the plastein reaction was 56.8% v/v, 5.26 kU/g peptide and 33.1C, respectively. The modified hydrolysates had better calcium‐chelating activities and stronger inhibition of calcium precipitation and platelet aggregation than SPH. The modified hydrolysate with the highest calcium‐chelating activity showed the strongest inhibitory effects on platelet aggregation and calcium precipitation. The plastein reaction enhances the in vitro calcium‐chelating and platelet anti‐aggregation activities of SPH. Practical Applications In this study, an alcalase‐catalyzed plastein reaction carried out in three media (ethanol–water, methanol–water and water) was used to modify the in vitro calcium‐chelating and platelet anti‐aggregation activities of an alcalase‐generated soy protein hydrolysate. The results revealed that the modified hydrolysates of higher calcium‐chelating activity had stronger inhibitory effects on platelet aggregation and calcium precipitation. The results of this study provide further insight on the enzymatic synthesis of bioactive peptides of higher activity using the plastein reaction.

Optimised condition for preparing sea cucumber ovum hydrolysate–calcium complex and its structural analysis

“…It has been reported that the Ca‐chelating capacity of WPH obtained at different hydrolysis periods ranged from 23.9 to 34.9 mg g −1 (Cai et al ., ). Zhang & Zhao () showed that soy protein hydrolysate generated by alcalase had a calcium‐chelating activity of 41 mg g −1 peptide. Hence, the SCOHs are suitable for producing peptide–calcium complexes.…”

Use of Alcalase in the production of bioactive peptides: A review

“…It has been reported that, when Alcalase is used to hydrolyze soy protein, the hydrolysate is rich in calcium-chelating activity, but if the reaction conditions are optimized J o u r n a l P r e -p r o o f using different media (water, ethanol-water, methanol-water), the calcium-chelating activities could be improved [564]. In another paper, casein and soybean proteins were hydrolyzed with Alcalase and trypsin [565].…”

Mechanisms of plastein formation, and prospective food and nutraceutical applications of the peptide aggregates

“…The antioxidative property of plastein was implicated in the cytoprotective activity of Phe- and Tyr-enriched plastein in H 2 O 2 - and galactosamine-induced damage to cultured rat hepatatocyte; the plastein increased cell viability and decreased malondialdehyde content and lactate dehydrogenase leakage associated with the hepatocyte damage [62] . Furthermore, plastein reaction was reported to improve the in vitro anticoagulation (inhibition of platelet aggregation) activity of soybean protein-derived plastein based on increased activated partial thromboplastin and prothrombin time [60] . These findings have added a new perspective to the application of plastein for the development of health-promoting products.…”