RESUMEN
The aim of this study is to characterize the bioactivity of mycelial biomass and crude exopolysaccharides (EPS) produced by Trametes versicolor NBIMCC 8939 and to reveal its nutraceutical potential. The EPS (1.58 g/L) were isolated from a culture broth. The macrofungal biomass was rich in protein, insoluble dietary fibers and glucans. The amino acid composition of the biomass was analyzed and 18 amino acids were detected. Three mycelial biomass extracts were prepared and the highest total polyphenol content (16.11 ± 0.14 mg GAE/g DW) and the total flavonoid content (5.15 ± 0.03 mg QE/g DW) were found in the water extract. The results indicated that the obtained EPS were heteropolysaccharides with glucose as the main building monosaccharide and minor amounts of mannose, xylose, galactose, fucose and glucuronic acid. Fourier Transform Infrared Spectroscopy (FTIR) confirmed the complex structure of the crude EPS. Five probiotic lactic acid bacteria strains were used for the determination of the prebiotic effect of the crude EPS. The anti-inflammatory potential was tested in vitro using cell line HT-29. The significant decrease of IL-1 and IL-8 and increase of TGF-beta expression revealed anti-inflammatory potential of the crude exopolysaccharides from T. versicolor.
RESUMEN
Members of the bacterial genus Bacillus are known as producers of a broad spectrum of antibiotic compounds of proteinaceous nature that possess inhibitory activity against different saprophytic and pathogenic microorganisms. In the current research, a peptide synthesized by Bacillus methylotrophicus strain BM47, previously isolated from a natural thermal spring in Bulgaria, was identified and characterized as a bacteriocin. In vitro antimicrobial screening of the crude bacteriocin substance of B. methylotrophicus BM47 showed activity against the plant pathogenic fungi Fusarium moniliforme, Aspergillus awamori, Penicillium sp., Aspergillus niger and Gram-negative bacterium Pseudomonas aeruginosa. The antimicrobial activity of the crude bacteriocin substance was partially inhibited by the enzymes trypsin, Alcalase®, Savinase®, proteinase K, papain and Esperase®, while catalase was not effective. The crude bacteriocin substance was relatively pH resistant, but sensitive to the action of heat and most organic solvents and detergents tested. To obtain the active protein fractions, crude bacteriocin substance was purified by fast protein liquid chromatography (FPLC) using a strong anion exchange column. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis demonstrated that the purified bacteriocin had molecular mass of 19 578 Da. The amino acid analysis performed by high-performance liquid chromatography (HPLC) revealed that the isolated bacteriocin consisted of 17 types of amino acids, with the highest mol fraction expressed as percent of serine (29.3), valine (10.3), alanine (9.8) and tyrosine (7.1).