The Protein Engineering of Zearalenone Hydrolase Results in a Shift in the pH Optimum of the Relative Activity of the Enzyme.

An acidic shift in the pH profile of zearalenone hydrolase (ZHD), the most effective and well-studied zearalenone-specific lactone hydrolase, is required to extend the range of applications for the enzyme as a decontamination agent in the feed and food production industries. Amino acid substitutions were engineered in the active center of the enzyme to decrease the pKa values of the catalytic residues E126 and H242. The T216K substitution provided a shift in the pH optimum by one unit to the acidic region, accompanied by a notable expansion in the pH profile under acidic conditions.

Transcriptomic Study of Treated with the Bacterial Protein CspD Reveals Some Specific Abiotic Stress Responses.

The ability of a cold-shock protein CspD from to protect both dicots and monocots against various pathogens is well confirmed under both greenhouse and field conditions; however, the molecular basis of this phenomenon at the transcriptomic level still remains unexplored. Expression profiles of some marker genes associated with SAR/ISR nonspecific resistance pathways and ROS scavengers were examined in CspD-treated plants, and the RNA-seq analysis of CspD-treated plants was first carried out. The ISR markers PDF1.

Cloning of Three Aflatoxin B1 Oxidases of the Dipeptidyl Peptidase III Family and Evaluation of Their Potential for Practical Applications as Decontamination Enzymes.

Aflatoxin B1 (AFB1) produced by some species belongs to the most dangerous contaminants of animal feeds. Development of safe and cost efficient decontamination methods saving feed quality and nutritional value are of paramount importance. The use of recombinant AFB1-detoxifying microbial enzymes represents a promising biotechnological approach meeting the aforementioned requirements.

Recombinant Oxidase from as a Potential Tool for Aflatoxin B1 Degradation in Contaminated Cereal Grain.

Forage grain contamination with aflatoxin B1 (AFB1) is a global problem, so its detoxification with the aim of providing feed safety and cost-efficiency is still a relevant issue. AFB1 degradation by microbial enzymes is considered to be a promising detoxification approach. In this study, we modified an previously developed GS115 expression system using a chimeric signal peptide to obtain a new recombinant producer of extracellular AFB1 oxidase (AFO) from (the yield of 0.