Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

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

Version 1 : Received: 29 March 2022 / Approved: 31 March 2022 / Online: 31 March 2022 (10:47:24 CEST)

A peer-reviewed article of this Preprint also exists.

Nguyen, T.H.; Wang, S.-L.; Nguyen, A.D.; Doan, M.D.; Tran, T.N.; Doan, C.T.; Nguyen, V.B. Novel α-Amylase Inhibitor Hemi-Pyocyanin Produced by Microbial Conversion of Chitinous Discards. Mar. Drugs 2022, 20, 283. Nguyen, T.H.; Wang, S.-L.; Nguyen, A.D.; Doan, M.D.; Tran, T.N.; Doan, C.T.; Nguyen, V.B. Novel α-Amylase Inhibitor Hemi-Pyocyanin Produced by Microbial Conversion of Chitinous Discards. Mar. Drugs 2022, 20, 283.

Journal reference: Mar. Drugs 2022, 20, 283
DOI: 10.3390/md20050283

Abstract

α-amylase inhibitors (aAIs) have been proved efficient for the management of type 2 diabetes. This study aimed to search the potential aAIs produced by microbial fermentation. Among various bacterial strains, Pseudomonas aeruginosa TUN03 was found as 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 the initial pH of 7-7.5, and fermentation was performed at 27.5 °C in 2 days. Further, aAIs compounds were investigated for scale-up production in a 14 L – bioreactor system, and the results highlighted high yield (4200 U/mL) in much shorter fermentation time (12 h) compared to fermentation in flasks. The bioactivity-guided purification resulted in the isolation of one major target compound. This active compound was confirmed as hemi-pyocyanin (HPC), with good purity, via using high-performance liquid chromatography and gas chromatography-mass spectrometry. Notably, HPC demonstrated potent activity comparable to acarbose, a commercial antidiabetic drug; this is the first-ever report of aAI activity of HPC. The docking study indicated that HPC inhibits α-amylase via 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-acceptor.

Keywords

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

Subject

BIOLOGY, Other

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