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Carbendazim (methyl benzimidazol-2-ylcarbamate: MBC) is a fungicide of the benzimidazole group that is widely used in the cultivation of pepper, ginseng, and many other crops. To remove the remnant carbendazim, many rhizobacteria are used as biodegradation agents. A bacterial strain of soil-isolated Bacillus velezensisHY-3479 was found to be capable of degrading MBC in M9 minimal medium supplemented with 250 mg/L carbendazim. The strain had a significantly higher degradation efficiency compared to the control strain Bacillus subtilisKACC 15590 in high-performance liquid chromatography (HPLC) analysis, and HY-3479 had the best degradation efficiency of 76.99% at 48 h. In gene expression analysis, upregulation of carbendazim-degrading genes (mheI, hdx) was observed in the strain. HY-3479 was able to use MBC as the sole source of carbon and nitrogen, but the addition of 12.5 mM NH4NO3significantly increased the degradation efficiency. HPLC analysis showed that the degradation efficiency increased to 87.19% when NH4NO3was added. Relative gene expression of mheIand hdxalso increased for samples with NH4NO3supplementation. The enzyme activity of the carbendazim-degrading enzyme and the 2-aminobenzimidazole-degrading enzyme was found to be highly present in the HY-3479 strain. It is the first reported B. velezensisstrain to biodegrade carbendazim (MBC). The biodegradation activity of strain HY-3479 may be developed as a useful means for bioremediation and used as a potential microbial agent in sustainable agriculture.

Alzheimer's disease (AD) is characterized by the age-related deposition of β-amyloid (Aβ) 40/42 peptide aggregates in vulnerable brain regions. Multiple levels of evidence implicate a central role for Aβ in the pathophysiology of AD. Aβ is generated by the regulated cleavage of a = 700 amino acid Aβ precursor protein (βAPP). Full-length βAPP can undergo proteolytic cleavage either within the Aβ domain to generate secreted sβAPPα or at the N-terminal and C-terminal domain(s) of Aβ to generate amyloidogenic Aβ peptides. Several epidemiological studies have reported that estrogen replacement therapy protects against the development of AD in postmenopausal women. The aim of this study was to elucidate the antioxidant neuroprotective mechanism of Bombusae concretioSalicea (BC). BC was effective protectants against oxidative glutamate toxicity in the murine neuroblastoma cells (N2a) and human neuroblastoma cells (SK-N-MC). BC exhibited similar protective properties against oxidative glutamate toxicity and H2O2toxicity. BC exhibited an antioxidant activity at approximately 20 μg/ml. BC of 5 μg/ml was ineffective in preventing the oxidative modification of LDL. The half-maximal effective concentration for BC was 16 μg/ml. These results suggested that BC supplementation in elderly men may be protective in the treatment of Alzheimer's disease (AD). We report here that treatment with BC increases the secretion of the nonamyloidogenic APP fragment, sβAPPα and decreases the secretion of Aβ peptides from N2a cells and rat primary cerebrocortical neurons. These results raise the possibility that BC supplementation in elderly men may be protective in the treatment of AD.

A gene encoding a chitin synthase with a myosin motor‐like domain (csm1) was isolated from Pyricularia oryzaeusing a PCR fragment amplified from a fungal chitin synthase conserved region. The deduced amino acid sequence of csm1is homologous to that of CsmA of Aspergillus nidulans(65% identity). The putative gene product of csm1is consisted of the myosin motor‐like domain and a chitin synthase domain as in A. nidulans csmA. The chitin synthase domain of its C‐terminus was also homologous to Aspergillus fumigatusChsE (61.4% identity) and Ustilago maydisChs6 (48.6% identity) that encode class V chitin synthases. Northern analysis demonstrated that the csm1was expressed throughout the mycelial growth of P. oryzae. This is the first report on the isolation of the gene encoding a class V chitin synthase with the myosin motor‐like domain from P. oryzae.

A gene encoding a chitin synthase with a myosin motor-like domain (csm1) was isolated from Pyricularia oryzae using a PCR fragment amplified from a fungal chitin synthase conserved region. The deduced amino acid sequence of csm1 is homologous to that of CsmA of Aspergillus nidulans (65% identity). The putative gene product of csm1 is consisted of the myosin motor-like domain and a chitin synthase domain as in A nidulans csmA. The chitin synthase domain of its C-terminus was also homologous to Aspergillus fumigatus ChsE (61.4% identity) and Ustilago maydis Chs6 (48.6% identity) that encode class V chitin synthases. Northern analysis demonstrated that the csm1 was expressed throughout the mycelial growth of P oryzae. This is the first report on the isolation of the gene encoding a class V chitin synthase with the myosin motor-like domain from P oryzae.