Novel bioactive peptides from red seaweed (Pyropia vietnamensis) proteins

Abstract

Abstract Pyropia vietnamensis is one of the most important and abundant seaweed in Indo-Pacific region. However, no study has been reported on the biotechnological utilization of this species. This study aimed to carry out in silico evaluation of P. vietnamensis proteins as potential precursors of bioactive peptides and to determine the most efficient proteolytic enzymes to release the bioactive peptides. In the present study, five main proteins from P. vietnamensis were chosen and analysed via in silico approach using the BIOPEP-UWM database. It was found that dipeptidyl peptidase-IV (DPP-IV) inhibitors and angiotensin-I converting enzyme (ACE) inhibitors were the most potential bioactive peptides released from P. vietnamensis proteins. Seven enzymes (pancreatic elastaste, papain, ficin, leukocyte elastaste, stem bromelain, calpain 2, and pepsin (pH>2)) were then employed for in silico proteolysis to release both dominant bioactivities. Pepsin (pH>2) and calpain 2 were found to be efficient in releasing a high number of fragments for both ACE and DPP-IV inhibitors. Two tripeptides (CFA, ACF) and five tetrapeptides (RFPS, DEWG, NYCL, CVPR, DACF) were screened as novel and promising bioactive peptides. PeptideRanker, PepCalc, Peptide Cutter, ToxinPred, AllerTop, and AHTpin were used to characterize the novel peptides. This study proposed that novel tetrapeptide of CVPR was the most potent bioactive peptides. This study proved that P. vietnamensis protein could serve as a precursor of bioactive peptides for further in vitro study.