Optimization of Preparation Process and Antioxidant Activity of Deer Bone Collagen Peptide in Vitro
In order to realize the high value-added utilization of deer bone,the present study was conducted to prepare deer bone collagen peptides by fermentation-enzymatic coupling technique.The fermentation process of deer bone was optimized using one-way and response surface tests with the removal rate of heteroproteins as an indicator,and then the collagen peptides of deer bone were prepared by enzymatic hydrolysis,and the fourier transform infrared spectroscopy(FT-IR),amino acid composition and antioxidant activity of the peptides were determined in vitro.The results showed that the optimal fermentation process conditions for deer bone were:fermentation time of 34.5 h,material-liquid ratio of 1∶26,and inoculation volume of 12％.Compared with unfermented deer bone collagen peptides(NCP),fermented deer bone collagen peptides(FCP)can be better hydrolyzed and have more amino acids related to antioxidation.The scavenging rates of the peptides on DPPH and ABTS free radicals were 55.84％and 95.11％respectively,and the IC50 values were 21.57 mg/mL and 0.19 mg/mL respectively.Meanwhile,the peptides were able to enhance the activities of antioxidant-related enzymes and down-regulate the levels of malondialdehyde(MDA),suggesting that they have antioxidant effect on aging human skin fibroblasts(HSF)cells induced by D-gal.and FCP has stronger antioxidant capacity than NCP.This study provides a theoretical basis for the deep exploitation and utilization of deer bone.
万方数据
维普
