Details

Autor(en) / Beteiligte

• Wei, Dong
• Fan, Wen-lai
• Xu, Yan

Titel

Identification of water-soluble peptides in distilled spent grain and its angiotensin converting enzyme (ACE) inhibitory activity based on UPLC-Q-TOF-MS and proteomics analysis

Ist Teil von

• Food chemistry, 2021-08, Vol.353, p.129521-129521, Article 129521

Ort / Verlag

England: Elsevier Ltd

Erscheinungsjahr

2021

Quelle

Access via ScienceDirect (Elsevier)

Beschreibungen/Notizen

• •22 Peptides were identified in distilled spent grain.•The angiotensin converting enzyme inhibitory activities of peptides was evaluated.•Targeted proteomics approach for peptide identification was firstly developed.•Pro-Arg was a competitive inhibitor of angiotensin converting enzyme. Distilled spent grain (DSG) is the biggest by-product in baijiu (Chinese liquor) production, releasing approximately 23.44 million tons every year. Aiming at comprehensive identification of more bioactive peptides, in this work, the new bioassay-guided proteomics and Biolynx peptide sequencer based on ultra-performance liquid chromatography quadrupole time-of-flight mass spectrometry (UPLC-Q-TOF-MS) were developed. Moreover, 22 peptides with angiotensin converting enzyme (ACE) inhibitory activities were identified. Seven peptides were successfully quantified using electrospray ionization with triple-quadrupole mass spectrometry (ESI-QQQ-MS) in the multiple reaction monitoring (MRM). Of these identified peptides, Pro-Arg was the most abundant (92.14 μg g−1 dry weight (DW)) and acted as a competitive inhibitor of ACE by molecular docking. Therefore, peptides from DSG can be considered as promising candidates for ACE inhibition; in addition, the new strategy for peptide sequencing can be extended to any food matrices containing peptide mixture or protein hydrolysate.