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Nematicidal activity of thermostable alkaline protease produced by Saccharomonospora viridis strain Hw G550.


ABSTRACT: Application of thermostable alkaline protease to control the harmful nematodes was investigated in the current study. A total of 14 proteolytic actinomycetes were isolated from Egyptian harsh environments. Out of them, isolate G550 exhibited the highest proteolytic activity (528.9 U/ml). Protease from isolate G550 exhibited high nematicidal activity against M. incognita under laboratory conditions and caused hydrolysis of J2S cuticle. This isolate was identified using molecular techniques and deposited in GenBank under name of Saccharomonospora viridis strain Hw G550 with accession number: MF152631. The G550 protease was extracted, characterized and applied under greenhouse conditions as nematicidal agent. This enzyme exhibited maximum activity and stability at alkaline pH (8) and thermal conditions (50-60?°C). Also, the results showed that, all treatments using protease caused a significant decrease in nematode reproduction and increasing in the plant properties. Finally, the thermo alkaliphilic protease could be used as bio-control agent against RKN.

SUBMITTER: Darwesh OM 

PROVIDER: S-EPMC6864322 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Nematicidal activity of thermostable alkaline protease produced by <i>Saccharomonospora viridis</i> strain Hw G550.

Darwesh Osama M OM   El-Hawary Ahmad S AS   El Kelany Usama S US   El-Sherbiny Gamal M GM  

Biotechnology reports (Amsterdam, Netherlands) 20191025


Application of thermostable alkaline protease to control the harmful nematodes was investigated in the current study. A total of 14 proteolytic actinomycetes were isolated from Egyptian harsh environments. Out of them, isolate G550 exhibited the highest proteolytic activity (528.9 U/ml). Protease from isolate G550 exhibited high nematicidal activity against <i>M. incognita</i> under laboratory conditions and caused hydrolysis of J<sub>2</sub>S cuticle. This isolate was identified using molecular  ...[more]

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