2. Academic Validation
  3. Novel α-Amylase Inhibitor Hemi-Pyocyanin Produced by Microbial Conversion of Chitinous Discards

Novel α-Amylase Inhibitor Hemi-Pyocyanin Produced by Microbial Conversion of Chitinous Discards

  • Mar Drugs. 2022 Apr 23;20(5):283. doi: 10.3390/md20050283.
Thi Hanh Nguyen 1 2,  San-Lang Wang 3 4,  Anh Dzung Nguyen 1,  Manh Dung Doan 1,  Thi Ngoc Tran 2,  Chien Thang Doan 2,  Van Bon Nguyen 1
Affiliations

Affiliations

  • 1 Institute of Biotechnology and Environment, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • 2 Department of Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam.
  • 3 Department of Chemistry, Tamkang University, New Taipei City 25137, Taiwan.
  • 4 Life Science Development Center, Tamkang University, New Taipei City 25137, Taiwan.
PMID: 35621934 DOI: 10.3390/md20050283
Abstract

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.

Keywords

diabetes; hemi-pyocyanin; marine discards; microbial conversion; α-amylase inhibitors.

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