Antifungal and antiaflatoxigenic mechanism activity of freeze-dried culture filtrate ofStreptomyces philanthiRL-1-178 on the two aflatoxigenic fungi and identification of its active component

Author:

Boukaew Sawai1,Zhang Zhiwei2,Prasertsan Poonsuk3,Igarashi Yasuhiro2

Affiliation:

1. College of Innovation and Management, Songkhla Rajabhat University , Songkhla 90000 , Thailand

2. Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University , Imizu, Toyama 9390398 , Japan

3. Research and Development Office, Prince of Songkla University , Hatyai, Songkhla 90112 , Thailand

Abstract

AbstractAimsThe study reports the antifungal and antiaflatoxigenic mechanism activity of freeze-dried culture filtrate of Streptomyces philanthi RL-1-178 (DCF RL-1-178) against two aflatoxigenic strains (Aspergillus parasiticus and A. flavus) and identification of its active component.Methods and ResultsSignificant inhibition in ergosterol biosynthesis by the DCF RL-1-178 appeared on the plasma membrane. Moreover, the DCF RL-1-178 showed dose-dependent inhibition of methylglyoxal (MG) (an aflatoxin inducer) biosynthesis and exhibited a novel antiaflatoxigenic action mechanism. Significant impairments in enzymatic [superoxide dismutase (SOD) and catalase (CAT)] and nonenzymatic [oxidized and reduced glutathione (GSH) and ratio of oxidized and reduced glutathione (GSSG)] anti-oxidative defense molecules were observed in the two aflatoxigenic cells. The active component of the DCF RL-1-178 was identified as natamycin. The natamycin exhibited against A. parasiticus and A. flavus with the minimum inhibitory concentration (MIC) values of 0.5 and 1.0 µg ml−1, respectively, while the minimum fungicidal concentration values were the same (4.0 µg ml−1).ConclusionsThe DCF RL-1-178 containing natamycin exhibited the following effects: (1) inhibition of cellular ergosterol biosynthesis on plasma membrane, (2) reduction in MG (aflatoxin inducer) confirmed novel antiaflatoxigenic mechanism of action, and (3) caused remarkable debasement in antioxidant defense enzymes (SOD and CAT) and nonenzymatic defense molecules (GSH and GSSG) revealing biochemical mechanism of action.

Funder

Agricultural Research Development Agency

Thailand Center of Excellence for Life Sciences

Publisher

Oxford University Press (OUP)

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology

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