Oenococcus oeni is a lactic acid bacterium involved in winemaking where it generally carries out the malolactic fermentation converting the wine's malic acid into lactic acid. In this work were used the strain m of Oenococcus oeni. The culture was inoculated at 10⁸ Log CFU/mL in a synthetic wine medium (SW) supplemented with a fraction of high molecular weight constituted by proteins and polypeptides (FPP) obtained from Cabernet Sauvignon and Syrah wines from Colalao del Valle, Tucumán, Argentine. In presence of FPP, O. oeni maintains viability after 48 h incubation time and release an extracellular proteolytic activity. Therefore, a release peptides of 1.247 and 1.373 mg N/L at 48 h of incubation time was detected in SW supplemented with FPP from Cabernet Sauvignon and Syrah wines respectively. Concomitantly with the maximum peptide release, the "in vitro" biological activities were increased. The released peptides from Cabernet Sauvignon wine enables the increase in the ferric reducing antioxidant power (FRAP) capacity, the scavenging activity of 2,2-diphenyl-1-picrylhydrazyl radical (DPPH), and the inhibition of angiotensin I-converting enzyme (ACEI activity) in 392.8 µmol FeSO₄/L, 9.7% and 63.9%, respectively. In presence of FPP of Syrah wine, the released peptides increases in 156.5 µmol FeSO₄/L, 5.5% and 13.8% the FRAP, DPPH and ACEI activities, respectively. The utilization of Oenococcus oeni m to carry out the malolactic fermentation would contribute to enhance the beneficial biological activities of the final product and provide an additional value to regional wines.
This chapter focuses on the non-isoprenoid alkyl derivatives of resorcinol, also known as alkylresorcinols (ARs), discussing their plant sources, methods of analysis, biological role in plants and microorganisms (e.g. plant-parasitic plant interaction and plant host-pathogen relationship), chemical properties, biological activities and their possible uses in nutrition, agriculture (plant protection) and industry.
The increase in biologically active peptides after proteolytic activity of Oenococcus oeni X 2 L was studied in grape juice medium (GJM) and in GJM fermented with Saccharomyces cerevisiae mc2. Sequential inoculation of O. oeni X 2 L with proteolytic activity in GJM before ("I" medium) and after ("F" medium) yeast fermentation allowed peptide release. In the "I" medium, bacterial proteolytic activity (0.083 mM) released 3.88 mg nitrogen (N) of peptides per liter and produced an increase of 203.39 µmol/L in the ferric reducing antioxidant power (FRAP) and 16.49% in the angiotensin I-converting enzyme inhibitory (ACE-I) activity after 48 hrs of incubation. In the "F" medium, a higher proteolytic activity was evidenced after 48 hrs of incubation (0.179 mM), releasing 0.87 mg N of peptides/L. The released peptides in the "F" medium produced an increase in ACE-I activity (22.15%). Calculation of the specific activity (activity expressed per mg N of peptide released) of FRAP, 1, 1-diphenyl-2-picrylhydrazyl scavenging, and ACE-I after 48 hrs of incubation revealed a higher activity in the "F" than in the "I" medium. This finding indicates a higher efficiency of the proteolytic system of O. oeni X 2 L on grape juice proteins in the release of bioactive peptides after yeast growth.
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