A comparative analysis of anti-lipidemic potential of soybean (Glycine max) protein hydrolysates obtained from different ripening stages: Identification, and molecular interaction mechanisms of novel bioactive peptides.

This study aims to investigate the potentials of mature (MSPHs) and young (YSPHs) soybean enzymatic protein hydrolysates for the inhibition of pancreatic lipase (PL) and cholesterol esterase (C-Ease) enzymes. Higher proteins degradation levels were recorded with Bromelain compared to Flavourzyme and Alcalase, and upon hydrolysis, improved PL and C-Ease inhibition performances were displayed compared to unhydrolyzed proteins. Afterwards, six PHs with potent anti-lipidemic activities were selected for sequencing using LC-MS QTOF and molecular binding studies. Peptides FPFPRPPHQ, QCCAFEM, FAPEFLK from MSPHs and SFFFPFELPRE, FMYL, PFLL, FPLL, LPHF from YSPHs were predicted to possess potent inhibitory activities against PL. Furthermore, FPFPRPPHQ, FMYL, MMLM from MSPHs, and SFFFPFELPRE from YSPHs were predicted to be potent inhibitors of C-Ease. FPFPRPPHQ and SFFFPFELPRE derived from MSPHs and YSPHs, respectively, demonstrated effective inhibition potentialities against both PL and C-Ease. Therefore, mature and young soybean-derived protein hydrolysates could be recognized as a potential ingredient in the management of hypercholesterolemia.

Characterization and identification of novel antidiabetic and anti-obesity peptides from camel milk protein hydrolysates.

In-vitro inhibitory properties of peptides released from camel milk proteins against dipeptidyl peptidase-IV (DPP-IV), porcine pancreatic α-amylase (PPA), and porcine pancreatic lipase (PPL) were studied. Results revealed that upon hydrolysis by different enzymes, camel milk proteins displayed dramatic increase in inhibition of DPP-IV and PPL, but slight improvement in PPA inhibition was noticed. Peptide sequencing revealed a total of 20 and 3 peptides for A9 and B9 hydrolysates respectively, obtained the score of 0.8 or more on peptide ranker and were categorized as potential DPP-IV inhibitory peptides. KDLWDDFKGL in A9 and MPSKPPLL in B9 were identified as most potent PPA inhibitory peptide. For PPL inhibition only 7 and 2 peptides qualified as PPL inhibitory peptides from hydrolysates A9 and B9, respectively. The present study report for the first time PPA and PPL inhibitory and only second for DPP-IV inhibitory potential of protein hydrolysates from camel milk.