Post-Harvest Prevention of Fusariotoxin Contamination of Agricultural Products by Irreversible Microbial Biotransformation: Current Status and Prospects.

Biological degradation of mycotoxins is a promising environmentally-friendly alternative to chemical and physical detoxification methods. To date, a lot of microorganisms able to degrade them have been described; however, the number of studies determining degradation mechanisms and irreversibility of transformation, identifying resulting metabolites, and evaluating in vivo efficiency and safety of such biodegradation is significantly lower. At the same time, these data are crucial for the evaluation of the potential of the practical application of such microorganisms as mycotoxin-decontaminating agents or sources of mycotoxin-degrading enzymes. To date, there are no published reviews, which would be focused only on mycotoxin-degrading microorganisms with the proved irreversible transformation of these compounds into less toxic compounds. In this review, the existing information about microorganisms able to efficiently transform the three most common fusariotoxins (zearalenone, deoxinyvalenol, and fumonisin B1) is presented with allowance for the data on the corresponding irreversible transformation pathways, produced metabolites, and/or toxicity reduction. The recent data on the enzymes responsible for the irreversible transformation of these fusariotoxins are also presented, and the promising future trends in the studies in this area are discussed.

Evaluation of eliciting activity of peptidil prolyl cys/trans isomerase from Pseudonomas fluorescens encapsulated in sodium alginate regarding plant resistance to viral and fungal pahogens.

Use of chemical pesticides poses a threat for environment and human health, so green technologies of crop protection are of high demand. Some microbial proteins able to activate plant defense mechanisms and prevent the development of resistance in plant pathogens, may be good alternative to chemicals, but practical use of such elicitors is limited due to need to protect them against adverse environment prior their delivery to target receptors of plant cells. In this study we examined a possibility to encapsulate heat resistant FKBP-type peptidyl prolyl cis-trans isomerase (PPIase) from Pseudomonas fluorescens, which possesses a significant eliciting activity in relation to a range of plant pathogens, in sodium alginate microparticles and evaluated the stability of resulted complex under long-term UV irradiation and in the presence of proteinase K, as well as its eliciting activity in three different "plant-pathogen" models comparing to that of free PPIase. The obtained PPIase-containing microparticles consisted of 70% of sodium alginate, 20% of bovine serum albumin, and 10% of PPIase. In contrast to free PPIase, which lost its eliciting properties after 8-h UV treatment, encapsulated PPIase kept its eliciting ability unchanged; after being exposed to proteinase K, its eliciting ability twice exceeded that of free PPIase. Using "tobacco-TMV", "tobacco-Alternaria longipes", and "wheat-Stagonospora nodorum" model systems, we showed that encapsulation process did not influence on the eliciting activity of PPIase. In the case of the "wheat-S. nodorum" model system, we also observed a significant eliciting activity of alginate-albumin complex and almost doubled activity of encapsulated PPIase as compared to the free PPIase. As far as we know, this is the first observation of a synergistic interaction between alginate and other compound possessing any bioactive properties. The results of the study show some prospects for a PPIase use in agriculture.