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Novel α-amylase inhibitor hemi-pyocyanin produced by microbial conversion of chitinous discards
25/05/23 09:08AM
Nguyen, Thi Hanh; San-Lang, Wang; Nguyen, Anh Dzung; Doan, Manh Dung; Tran, Thi Ngoc; et al.  Marine Drugs; Basel Vol. 20, Iss. 5, (2022): 283. DOI:10.3390/md20050283


α-Amylase inhibitors (aAIs) have been applied for the efficient management of type 2 diabetes. The aim of this study was to search for potential aAIs produced by microbial fermentation. Among various bacterial strains, Pseudomonas aeruginosa TUN03 was found to be a potential aAI-producing strain, and shrimp heads powder (SHP) was screened as the most suitable C/N source for fermentation. P. aeruginosa TUN03 exhibited the highest aAIs productivity (3100 U/mL) in the medium containing 1.5% SHP with an initial pH of 7–7.5, and fermentation was performed at 27.5 °C for two days. Further, aAI compounds were investigated for scaled-up production in a 14 L-bioreactor system. The results revealed a high yield (4200 U/mL) in a much shorter fermentation time (12 h) compared to fermentation in flasks. Bioactivity-guided purification resulted in the isolation of one major target compound, identified as hemi-pyocyanin (HPC) via gas chromatography-mass spectrometry and nuclear magnetic resonance. Its purity was analyzed by high-performance liquid chromatography. HPC demonstrated potent α-amylase inhibitory activity comparable to that of acarbose, a commercial antidiabetic drug. Notably, HPC was determined as a new aAI. The docking study indicated that HPC inhibits α-amylase by binding to amino acid Arg421 at the biding site on enzyme α-amylase with good binding energy (−9.3 kcal/mol) and creating two linkages of H-acceptors.

Fulltext: https://doi.org/10.3390/md20050283

(Source: https://www.proquest.com/scholarly-journals/novel-α-amylase-inhibitor-hemi-pyocyanin-produced/docview/2670356626/se-2?accountid=28030)