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1.
Appl Microbiol Biotechnol ; 102(1): 511, 2018 01.
Article in English | MEDLINE | ID: mdl-29159584

ABSTRACT

After publication of the original article, authors found that there has been a minor mistake in the units of kcat and kcat/Km in Table 2. The units should be 103 min-1 g-1 FAE for kcat and mM-1 min-1 g-1 FAE for kcat/Km. This correction does not affect any conclusions drawn within the article.

2.
Appl Microbiol Biotechnol ; 101(8): 3213-3226, 2017 Apr.
Article in English | MEDLINE | ID: mdl-28078397

ABSTRACT

Five feruloyl esterases (FAEs; EC 3.1.1.73), FaeA1, FaeA2, FaeB1, and FaeB2 from Myceliophthora thermophila C1 and MtFae1a from M. thermophila ATCC 42464, were tested for their ability to catalyze the transesterification of vinyl ferulate (VFA) with prenol in detergentless microemulsions. Reaction conditions were optimized investigating parameters such as the medium composition, the substrate concentration, the enzyme load, the pH, the temperature, and agitation. FaeB2 offered the highest transesterification yield (71.5 ± 0.2%) after 24 h of incubation at 30 °C using 60 mM VFA, 1 M prenol, and 0.02 mg FAE/mL in a mixture comprising of 53.4:43.4:3.2 v/v/v n-hexane:t-butanol:100 mM MOPS-NaOH, pH 6.0. At these conditions, the competitive side hydrolysis of VFA was 4.7-fold minimized. The ability of prenyl ferulate (PFA) and its corresponding ferulic acid (FA) to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radicals was significant and similar (IC50 423.39 µM for PFA, 329.9 µM for FA). PFA was not cytotoxic at 0.8-100 µM (IC50 220.23 µM) and reduced intracellular reactive oxygen species (ROS) in human skin fibroblasts at concentrations ranging between 4 and 20 µM as determined with the dichloro-dihydro-fluorescein diacetate (DCFH-DA) assay.


Subject(s)
Carboxylic Ester Hydrolases/metabolism , Coumaric Acids/metabolism , Pentanols/metabolism , Sordariales/enzymology , Antioxidants , Carboxylic Ester Hydrolases/isolation & purification , Cells, Cultured , Coumaric Acids/pharmacology , Emulsions , Esterification , Fibroblasts/drug effects , Fibroblasts/metabolism , Hemiterpenes , Humans , Hydrogen-Ion Concentration , Kinetics , Reactive Oxygen Species/metabolism , Sordariales/metabolism , Temperature
3.
Redox Biol ; 5: 205-215, 2015 Aug.
Article in English | MEDLINE | ID: mdl-25974626

ABSTRACT

Despite the fact that several natural products (e.g. crude extracts or purified compounds) have been found to activate cell antioxidant responses and/or delay cellular senescence the effect(s) of small peptides on cell viability and/or modulation of protective mechanisms (e.g. the proteostasis network) remain largely elusive. We have thus studied a hexapeptide (Hexapeptide-11) of structure Phe-Val-Ala-Pro-Phe-Pro (FVAPFP) originally isolated from yeast extracts and later synthesized by solid state synthesis to high purity. We show herein that Hexapeptide-11 exhibits no significant toxicity in normal human diploid lung or skin fibroblasts. Exposure of fibroblasts to Hexapeptide-11 promoted dose and time-dependent activation of proteasome, autophagy, chaperones and antioxidant responses related genes. Moreover, it promoted increased nuclear accumulation of Nrf2; higher expression levels of proteasomal protein subunits and increased proteasome peptidase activities. In line with these findings we noted that Hexapeptide-11 conferred significant protection in fibroblasts against oxidative-stress-mediated premature cellular senescence, while at in vivo skin deformation assays in human subjects it improved skin elasticity. Finally, Hexapeptide-11 was found to induce the activity of extracellular MMPs and it also suppressed cell migration. Our presented findings indicate that Hexapeptide-11 is a promising anti-ageing agent.


Subject(s)
Oligopeptides/pharmacology , Oxidative Stress/drug effects , Antioxidants/metabolism , Autophagy/drug effects , Cell Line , Cell Movement/drug effects , Cell Survival/drug effects , Cellular Senescence/drug effects , Diploidy , Fibroblasts/cytology , Fibroblasts/metabolism , Humans , Matrix Metalloproteinase 2/metabolism , Matrix Metalloproteinase 9/metabolism , Molecular Chaperones/genetics , Molecular Chaperones/metabolism , NF-E2-Related Factor 2/metabolism , Proteasome Endopeptidase Complex/genetics , Proteasome Endopeptidase Complex/metabolism
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