A Peptidomics-Based Approach to Screen Strains for Enhanced Dipeptidyl Peptidase IV Inhibition in Tilapia (Oreochromis mossambicus) Skin
摘要
Based on the screening of microbial strains for efficient production of dipeptidyl peptidase Ⅳ (DPP-IV) inhibitory peptides from tilapia (Oreochromis mossambicus) skin, this study evaluated the fermentation characteristics of 12 strains from the genera Bacillus subtilis, Bacillus licheniformis, and Aspergillus oryzae. The results indicated that the fermentation broths of B. subtilis ATCC 21332 and B. licheniformis ATCC 21424 exhibited the highest DPP-IV inhibition rates, at 72.59 ± 3.17% and 71.74 ± 1.22%, respectively, significantly superior to that of A. oryzae CGMCC 3.951. Peptidomics and in silico analyses revealed that the proportion of potential inhibitory peptides was highest in the fermentation broths of two Bacillus strains. A key structural feature of these peptides was the prevalence of hydrophobic amino acids are the first or second N-terminal position, which was a critical characteristic closely associated with DPP-IV inhibitory activity. Further cleavage site analysis demonstrated that the enzymatic specificity of the two Bacillus strains enabled more efficient production of peptides possessing this structural feature. In vitro experiments confirmed that the inhibitory peptides produced by the two Bacillus strains surpassed those of A. oryzae in both quantity and activity. Notably, the LAPGGHVGA derived from B. subtilis and FAPVNLTTE derived from B. licheniformis exhibited excellent inhibitory activity, with IC50 values of 719 ± 134 µM and 717 ± 77 µM, respectively. Therefore, B. subtilis ATCC 21332 and B. licheniformis ATCC 21424 exhibited potential as microbial strains to enhance DPP-IV inhibitory action in fermented tilapia skin.
Graphical Abstract