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Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique
Published on: July 19, 2019
Identification of water-soluble peptides in distilled spent grain and its angiotensin converting enzyme (ACE)
Dong Wei1, Wen-Lai Fan1, Yan Xu1
1Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, 1800 Lihu Avenue, Wuxi, Jiangsu 214122, China; Laboratory of Brewing Microbiology and Applied Enzymology, School of Biotechnology, Jiangnan University, Wuxi 214000, Jiangsu, China.
Abstract:
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.

