Journal
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
Volume 181, Issue 1, Pages 48-64Publisher
HUMANA PRESS INC
DOI: 10.1007/s12010-016-2198-1
Keywords
Fermentation; Bioactive peptides; Size exclusion chromatography; MALDI-TOF
Funding
- Ministry of Science, Research and Technology of Iran
- Emerging Research Group Grant from Generalitat Valenciana of Spain [GV/2015/138]
- JAEDOC-CSIC postdoctoral contract
- European Social Fund
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The effects of amino acid composition and peptide molecular mass on ACE-inhibitory and antioxidant activities of protein fragments obtained from tomato waste fermented using Bacillus subtilis were evaluated. The addition of B. subtilis increased the relative amounts of aromatic and positively-charged amino acids which have been described to influence the biological activities of peptide fragments. IC50 values of hydrolysates for ACE-inhibitory and 2, 2'-diphenyl-1-picrylhydrazyl (DPPH) scavenging activities were found to be 1.5 and 8.2 mg/mL, respectively. Size-exclusion chromatography (SEC) pattern of the hydrolysate indicated the breakdown of parent proteins to smaller peptides with molecular weights mainly below 1400 Da. MALDI-TOF mass spectrometry analysis revealed that the highest ACE-inhibitory activity was due to peptides showing molecular mass range 500-800 Da, while the most active antioxidant peptides were found to be mainly at the two different peptide weight ranges 500-800 Da and 1200-1500 Da.
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