Dipeptidyl Peptidase-IV Inhibitory Activity of Peptides in Porcine Skin Gelatin Hydrolysates

Screening and identification of DPP-IV inhibitory peptides from deer skin hydrolysates by an integrated approach of LC–MS/MS and in silico analysis

“…A systematic study of the mechanisms through which peptide modifications affect the inhibition of DPP-IV will be of benefit to those exploring novel DPP-IV inhibitory peptides from proteins. Previous studies regarding DPP-IV inhibitory peptides focused on short peptides with two to seven amino acids using empirical approaches (Hatanaka, Kawakami, & Uraji, 2014;Hsu et al, 2013;Lafarga et al, 2014) or in silico approaches (Lacroix & Li-Chan, 2012b). Although larger peptides with 13 amino acids have been reported to possess DPP-IV inhibitory activity (Velarde-Salcedo et al, 2013), the effect of the peptide length on DPP-IV inhibition has rarely been discussed.The DPP-IV inhibitory peptides identified in the present study contain nine to eleven amino acids.…”

“…The DPP-IV inhibition assay was performed in 96-well microplates as described previously (Hsu et al, 2013). The lyophilized hydrolysates or peptides were dissolved in 0.1 M TrisHCl buffer (pH 8.0) at concentrations ranging from 0.25 to 10 mg mL −1 or 12.5 to 500 μg mL −1 , respectively.…”

“…Peptides with various activities have been identified from hydrolysates of fish gelatin Alemán, Giménez, Pérez-Santin, Gómez-Guillen, & Montero, 2011;Byun & Kim, 2001;Li-Chan et al, 2012;Mendis, Rajapakse, & Kim, 2005;Uriarte-Montoya et al, 2011), bovine gelatin (Kim, Kim, & Leem, 2014), porcine gelatin (Hsu, Tung, Huang, & Jao, 2013;Li, Chen, Wang, Ji, & Wu, 2007), and chicken collagen (Saiga et al, 2008). It is well known that the dominant sequence of collagen is a continuous repeating sequence of Gly-X-Y triplets, where X is mostly proline and Y is mostly hydroxyproline (Asghar & Henrickson, 1982).…”

Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase‐IV inhibitors

“…FAN values of NC hydrolysates were significantly higher (p < .05) than those of CP and β-Lg hydrolysates (Figure 4). Leu, Val or Phe (Hsu et al, 2013). Consequently, the proteases would have limited access to peptide bonds in CP compared with NC, which are more soluble in water and hence available for hydrolysis.…”

“…Many hydrophobic amino acids are found in potent DPP-IV inhibiting peptides(Hsu, Tung, Huang, & Jao, 2013), as they facilitate peptide binding to hydrophobic pockets of the enzyme active site. This information guided wet laboratory processing of the edible insect larvae.…”