Antifungal proteins produced by molds are generally small, highly basic, and cysteine-rich. The best known effects of these proteins include morphological changes, metabolic inactivation, and membrane perturbation on sensitive fungi. Reactive oxygen species (ROS) generation leads to apoptosis, with G -protein playing a key role in transduction of cell death signals. The antifungal protein PgAFP from Penicillium chrysogenum inhibits growth of some toxigenic molds. Here we analyzed the effect of the antifungal protein PgAFP on the growth of Aspergillus flavus. For this, comparative proteomic analysis was used to identify the whole protein profile and protein change in abundance after PgAFP treatment. PgAFP provoked metabolic changes related to reduced energy metabolism, cell wall integrity alteration, and increased stress response due to higher levels of ROS. The observed changes in protein abundance, favoring a higher glutathione concentration as well as the increased abundance in heat shock proteins, do not seem to be enough to avoid necrosis. The decreased chitin deposition observed in PgAFP-treated A. flavus is attributed to a lower relative quantity of Rho1. The reduced relative abundance of a β subunit of G -protein seems to be the underlying reason for modulation of apoptosis in PgAFP-treated A. flavus hyphae. We propose Rho1 and G -protein subunit β CpcB to be the main factors in the mode of action of PgAFP in A. flavus. Additionally, enzymes essential for the biosynthesis of aflatoxin were no longer detectable in A. flavus hyphae at 24 h, following treatment with PgAFP. This presents a promising effect of PgAFP, which may prevent A. flavus from producing mycotoxins. However, the impact of PgAFP on actual aflatoxin production requires further study.

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IO . 1998. In order to determine the possible contribution of micro-organisms to the ripening of meat products, 48 cocci, 18 moulds and 20 yeasts isolated from dry-cured Iberian ham were evaluated for proteolytic activity. Two specific methods were used: the ability to hydrolyse myosin in broth and, for those strains showing high activities, hydrolysis on both myofibrillar and sarcoplasmic proteins on pork slices. Moulds and cocci showed the highest proteolytic activity for myosin in broth. Both myofibrillar and sarcoplasmic proteins were recovered at lower rates from inoculated than from sterile incubated pork. The deepest changes in myofibrillar and sarcoplasmic proteins were originated by one strain each of Penicillium chrysogenum and Staphylococcus xylosus, respectively. Only small changes were observed in the concentrations of free amino acids from inoculated pork slices, except for the samples with P. chrysogenum, where there were increases in all free amino acids. Thus, P. chrysogenum makes a significant contribution to proteolysis during the ripening of dry-cured meat products.

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