Abstract

Peptides show biological activity, and are more easily digested than complex proteins. In the present work, we evaluated the effects of soy hydrolysate on skeletal muscle. Soy protein isolate (SPI) was hydrolysed using 2% Alcalase (SPHA) and Flavourzyme (SPHF) at pH 8 for 3 h at 60°C, and at pH 7 for 3 h at 55°C, respectively. Antioxidant properties (total phenolic content and DPPH activity) and inhibition of muscle loss (myogenin, myosin heavy chain [MyHC], creatine kinase, and myostatin) by the SPI hydrolysates in C2C12 cells were compared with those of SPI. Alcalase produced more hydrolysed soy oligopeptides than Flavourzyme. Enzymatic hydrolysis increased the levels of essential amino acids, particularly in SPHF (2,466.85 mg/L) as compared to SPI (56.08 mg/L). The total phenolic contents of hydrolysates increased from 12.02 mg GAE/g in SPI to 22.87 and 18.67 mg GAE/g in SPHA and SPHF, respectively. The IC50 value of DPPH activity decreased four times after hydrolysis (SPI: 124.38, SPHA: 32.18, and SPHF: 30.21 mg/mL). SPHA and SPHF treatments increased the expression levels of both MyHC1 and MyHC3, as well as creatine kinase activity. A significant increase in MyHC3 expression was observed in SPHF at 10 µg/mL. Soy hydrolysates (SPHA: 93.5% and SPHF: 61%) induced a greater decrease in the expression of myostatin, a muscle reduction marker, than SPI (30.4%). In conclusion, soy hydrolysates may inhibit muscle loss, showing particularly better effects when Alcalase is used for hydrolysis.

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