Study on coffee quality improvement by self-induced anaerobic fermentation: Microbial diversity and enzymatic activity.

The postharvest fermentation process of coffee has rapidly advanced in the last few years due to the search for quality and diversity of sensorial profiles. A new type of fermentation, named self-induced-anaerobic fermentation (SIAF), is a promising process that has been increasingly used. This study aims to evaluate the sensorial improvement of coffee beverages during SIAF and the influence of microorganism's community and enzymatic activity. The SIAF process was conducted in Brazilian farms for up to 8 days. The sensorial quality of coffee was evaluated by Q-graders; the microbial community was identified by the high-throughput sequencing of 16S rRNA and ITS regions; and the enzymatic activity (invertase, polygalacturonase, and endo-ß-mannanase) was also investigated. SIAF increased up to 3.8 points in the total score of sensorial evaluation (compared to the non-fermented sample), in addition to presenting more flavor diversity (especially within the fruity and sweetness descriptors). The high-throughput sequencing identified 655 bacterial and 296 fungal species during the three processes. The bacteria Enterobacter sp., Lactobacillus sp., Pantoea sp., and the fungi Cladosporium sp. and Candida sp. were the predominant genera. Fungi that are potential producers of mycotoxin were identified throughout the process, which indicates a risk of contamination since some of them are not degraded in the roasting process. Thirty-one species of microorganisms were described for the first time in coffee fermentation. The microbial community was influenced by the place where the process was carried out, mainly in relation to the diversity of fungi. Washing the coffee fruits before fermenting led to a fast reduction of pH; a fast development of Lactobacillus sp. and a fast dominance of Candida sp.; a reduction of the fermentation time necessary to achieve the best sensorial score; an increase in the invertase activity in the seed; a more expressive invertase activity in the husk; and a decreasing trend in polygalacturonase activity in the coffee husk. The increase in endo-ß-mannanase activity suggests that coffee starts germinating during the process. SIAF has a huge potential to increase the quality and add value to coffee, but further studies must be conducted to access its safety. The study allowed a better knowledge of the spontaneous microbial community and the enzymes that were present in the fermentation process.

Phosphoprotein levels, MAPK activities and NFkappaB expression are affected by fisetin.

Flavonoids, polyphenolic phytochemicals, are ubiquitous in plants and are commonly present in the human diet. They may exert diverse beneficial effects, including antioxidant and anticarcinogenic activities. The present study was designed to evaluate three biomolecules that play important roles in the apoptotic process: mitogen-activated protein kinases, protein phosphatases and NFkappaB, using HL60 cells treated with fisetin as an experimental model. Our results demonstrated that cells treated with fisetin presented high expression of NFkappaB, activation of MAPK p38 and an increase of phosphoprotein levels; inhibition of enzymes involved in redox status maintenance were also observed. Our findings reinforce the hypothesis that fisetin is likely to exert beneficial and/or toxic actions on cells not through its potential as antioxidant but rather through its modulation of protein kinase and phosphatase signaling cascades. Additionally, our results also indicate that the cellular effects of fisetin will ultimately depend on the cell type and on the extent to which they associate with the cells, either by interactions at the membrane or by uptake into the cytosol.

Effect of homologous series of n-alkyl sulfates and n-alkyl trimethylammonium bromides on low molecular mass protein tyrosine phosphatase activity.

The effect of anionic and cationic surfactants on acid phosphatase denaturation has been extensively studied. Low molecular mass (LMr) protein tyrosine phosphatase (PTP), a key regulatory enzyme involved in many different processes in the cell, was distinctly affected by anionic (homologous series of n-alkyl sulfates (C8-C14)) and cationic (n-alkyl trimethylammonium bromides (C12-C16)) surfactants. At concentrations 10-fold lower critical micellar concentration (cmc) values, the enzyme was completely inactivated in the presence of anionic surfactants, in a process independent of the pH, and dependent on the chain length of the surfactants. Under the same conditions, the effect of cationic surfactants on the enzyme activity was pH-dependent and only at pH 7.0 full inactivation was observed at concentrations 10-fold higher cmc values. In contrast to cationic surfactants the effect of anionic surfactants on the enzyme activity was irreversible and was not affected by the presence of NaCl. Inorganic phosphate, a known competitive inhibitor of PTP, protected the enzyme against inactivation by the surfactants. Our results suggest that the inactivation of the LMr PTP by anionic and cationic surfactants involved both electrostatic and hydrophobic interactions, and that the interactions enzyme-surfactants probably occurred at or near the active site.