Biosynthesis of Cry5B-Loaded Sulfur Nanoparticles using Arthrobotrys oligospora Filtrate Effects on Nematicidal Activity Thermal Stability and Pathogenicity against Caenorhabditis elegans
Biosynthesis of Cry5B-Loaded Sulfur Nanoparticles using Arthrobotrys oligospora Filtrate Effects on Nematicidal Activity Thermal Stability and Pathogenicity against Caenorhabditis elegans
Author
Jammor P. Sanguanphun T. Meemon K. Promdonkoy B. Boonserm P.
Affiliations
Institute of Molecular Biosciences Mahidol University Phuttamonthon Salaya Nakhon Pathom 73170 Thailand; Department of Anatomy Faculty of Science Mahidol University Rama VI Road Bangkok 10400 Thailand; National Center for Genetic Engineering and Biotechnology National Science and Technology Development Agency 113 Phahonyothin Road Pathumthani Khlong Luang 12120 Thailand
Type
Article
Source Title
ACS Omega
ISSN
24701343
Year
2024
Volume
9
Issue
6
Page
6945-6954
Open Access
All Open Access Gold
Publisher
American Chemical Society
DOI
10.1021/acsomega.3c08653
Abstract
Cry5B a crystal protein produced by Bacillus thuringiensis (Bt) is a bionematicide with potent nematicidal activity against various plant-parasitic and free-living nematodes. This protein however is susceptible to destruction by ultraviolet light proteolytic enzymes and high temperatures. This study aims to produce Cry5B protein for bionematicidal use and improve its stability and nematicidal efficacy by loading it intoArthrobotrys oligospora-mediated sulfur nanoparticles (AO-SNPs). Based on the mortality assay the Cry5B protein exhibited dose-dependent nematicidal activity against the model organismCaenorhabditis elegans. The nematicidal activity thermal stability and pathogenic effects of Cry5B-loaded AO-SNPs (Cry5B-SNPs) were compared to those of free Cry5B. After 3 h of exposure to heat at 60 ?C Cry5B-SNPs had greater nematicidal activity than free Cry5B protein indicating the effective formulation of Cry5B-SNPs that could be used as an alternative to current nematicide delivery strategies. ? 2024 The Authors. Published by American Chemical Society.
