Controlled Enzymatic Hydrolysis of Egg Yolk Protein and the Pro-osteoblast Proliferative Activity of the Resulting Hydrolysate
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Abstract:
Defatted egg yolk powder is as a byproduct of the industrial extraction of egg yolk lecithin. This protein and nutrient-rich product appears to be commercially valuable. To optimize enzymatic hydrolysis, defatted egg yolk powder samples were hydrolyzed using trypsin, with calcium chelating capacity serving as the primary evaluation index. The optimum hydrolysis conditions were identified by coupling unidirectional analysis (involving variables like hydrolysis duration, temperature, pH, and enzyme dosage) to response surface optimization. The pro-proliferative activity of the resulting hydrolysate in the context of MC3T3-E1 osteoblasts was assessed to enable the high-value application of defatted egg yolk powder. The results indicated that under optimum conditions, i.e., hydrolysis duration, 3 h; temperature, 55 ℃; pH, 10.0; enzyme dosage, 1%, the calcium chelating capacity reached 87.12%. The hydrolysate produced under these conditions markedly enhanced the proliferation of MC3T3-E1 osteoblasts. This enhancement was most pronounced at a hydrolysate concentration of 1.00 mg/mL, where the proliferation of the treatment group osteoblasts was more than that of the blank group osteoblasts (by 1.20 times). The findings of this study reveal that the trypsin-facilitated enzymatic hydrolysis of defatted egg yolk powder effectively produces hydrolysates with considerable pro-osteoblast proliferative activity, thereby supporting the high-value application of defatted egg yolk powder.
