Research opportunities: Traditional fermented beverages in Mexico. Cultural, microbiological, chemical, and functional aspects.

In Mexico, close to 200 fermented products have been described, of which, approximately 20 are beverages. They were obtained through rustic and ancestral fermentation methods by different indigenous Mexican communities; most of them were used in ceremonies, agricultural work, and other occasions. For their elaboration, different substrates obtained from plants are used, where uncontrolled and low-scale spontaneous anaerobic fermentation occurs. In Mexico, some of these products are considered as nutritional sources and functional beverages; the study of those products has revealed the presence of multiple compounds of biological importance. Additionally, elder generations attribute healing properties against diverse illnesses to these beverages. The aim of this review is to highlight the available information on twelve traditional Mexican fermented beverages, their traditional uses, and their fermentation processes along with toxicological, chemical, nutritional, and functional studies as seen from different areas of investigation. In the literature, pulque, cocoa, and pozol were the beverages with the greatest amount of described health properties; sendechó and guarapo were less characterized. Polyphenols, gallic and ferulic acid, anthocyanins and saponins were the most abundant molecules in all beverages. Finally, it is important to continue this research in order to determine the microorganisms that are involved in the fermentation process, as well as the organoleptic and beneficial properties they lend to the traditional Mexican fermented beverages.

Involvement of the amino-terminal beta-hairpin of the Aspergillus ribotoxins on the interaction with membranes and nonspecific ribonuclease activity.

Ribotoxins are a family of potent cytotoxic proteins from Aspergillus whose members display a high sequence identity (85% for about 150 amino acid residues). The three-dimensional structures of two of these proteins, alpha-sarcin and restrictocin, are known. They interact with phospholipid bilayers, according to their ability to enter cells, and cleave a specific phosphodiester bond in the large subunit of ribosome thus inhibiting protein biosynthesis. Two nonconservative sequence changes between these proteins are located at the amino-terminal beta-hairpin of alpha-sarcin, a characteristic structure that is absent in other nontoxic structurally related microbial RNases. These two residues of alpha-sarcin, Lys 11 and Thr 20, have been substituted with the equivalent amino acids in restrictocin. The single mutants (K11L and T20D) and the corresponding K11L/T20D double mutant have been produced in Escherichia coli and purified to homogeneity. The spectroscopic characterization of the purified proteins reveals that the overall native structure is preserved. The ribonuclease and lipid-perturbing activities of the three mutants and restrictocin have been evaluated and compared with those of alpha-sarcin. These proteins exhibit the same ability to specifically inactivate ribosomes, although they show different activity against nonspecific substrate analogs such as poly(A). The mutant variant K11L and restrictocin display a lower phospholipid-interacting ability correlated with a decreased cytotoxicity. The results obtained are interpreted in terms of the involvement of the amino-terminal beta-hairpin in the interaction with both membranes and polyadenylic acid.