BACKGROUND Bioinformatics approaches are widely used to evaluate the prospects of novel protein sources in bioactive peptide research. Edible cyanobacteria are considered as potential protein precursors. However, the abundance of… Click to show full abstract
BACKGROUND Bioinformatics approaches are widely used to evaluate the prospects of novel protein sources in bioactive peptide research. Edible cyanobacteria are considered as potential protein precursors. However, the abundance of unicellular cyanobacterial proteins is largely unknown and highly dynamic according to the cultivation conditions, which need to be considered in this research field. The objective of this work was to evaluate the protein abundance of Arthrospira platensis, as well as to map the bioactive peptide sequences from the high-abundance proteins of the A. platensis proteome. RESULTS The high-abundance proteins of the A. platensis proteome were identified with a high-performance liquid chromatography-tandem mass spectrometry-based method. A total of 593 proteins were detected and quantified. The occurrence frequency of the bioactive peptides in A. platensis proteome was calculated according to the amino acid sequences via the bioinformatics approaches. Further in silico digested by trypsin, pepsin and chymotrypsin, these proteins liberated 78, 99, and 96 bioactive peptides, respectively. In each case, angiotensin-converting enzyme inhibitors and dipeptidyl peptidase IV inhibitors were enriched. CONCLUSION This work will help rationally design the protocols for cyanobacterial cultivation, protein pre-treatment and peptide separation, and further produce more peptides with specific functions. © 2017 Society of Chemical Industry.
               
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