Publications by authors named "Nguyen Hoang Tue"
Article Synopsis
- The study aimed to purify a 42 kDa chitinase from Trichoderma asperellum SH16, produced in Nicotiana benthamiana, using a PEG/salt aqueous two-phase system.
- The optimal partitioning conditions identified were 300 g/L PEG 6000 combined with potassium phosphate (PP) showing better efficiency than sodium phosphate (SP), resulting in higher enzymatic activity after purification.
- The purified chitinase demonstrated significant antifungal activity against Sclerotium rolfsii, indicating its potential for use in agriculture and preserving fruits and vegetables postharvest.
Chitinases are enzymes that catalyze the degradation of chitin, a major component of the cell walls of pathogenic fungi and cuticles of insects, gaining increasing attention for the control of fungal pathogens and insect pests. Production of recombinant chitinase in a suitable host can result in a more pure product with less processing time and a significantly larger yield than that produced by native microorganisms. The present study aimed to express the synthetic chi42 gene (syncodChi42), which was optimized from the chi42 gene of Trichoderma asperellum SH16, in Escherichia coli to produce 42 kDa chitinase (Ta-CHI42); then determined the activity of this enzyme, characterizations and in vitro antifungal activity as well as its immunogenicity in mice.
View Article and Find Full Text PDFThe present study reports on the cloning, expression and characterization of catechol 1,2-dioxygenase (CAT) of bacterial strains isolated from dioxin-contaminated soils in Vietnam. Two isolated bacterial strains DF2 and DF4 were identified as Burkholderia cepacia based on their 16S rRNA sequences. Their genes coding CAT was amplified with a specific pair of primers.
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