Impact of lactic acid fermentation on acids, sugars, and phenolic compounds in black chokeberry and sea buckthorn juices.

The aim of this research was to study the potential of malolactic fermentation to modify the composition of the juices of sea buckthorn, chokeberry and lingonberry. Juices were prepared with and without pectinolytic enzyme treatment, followed by fermentation with commercially available strains of Lactobacillus plantarum, originally isolated from fermented plant materials. The juices before and after the fermentation were analyzed with GC-FID, HPLC-DAD, and HPLC-MS. Enzyme treatment significantly increased the phenolic content in the juices by 11-50%. None of strains showed ability to ferment lingonberry juice. On the other hand, L. plantarum DSM 10492 and DSM 20174 converted all malic acid to lactic acid in sea buckthorn and chokeberry juices, respectively. Fermentation with DSM 10492 reduced the content of flavonols by 9-14% and hydroxycinnamic acids by 20-24% in chokeberry juice. Flavonol glycosides and sugars in sea buckthorn as well as anthocyanins in chokeberry remained unaffected by the fermentation.

Comparison and applications of label-free absolute proteome quantification methods on Escherichia coli.

Three different label-free proteome quantification methods--APEX, emPAI and iBAQ--were evaluated to measure proteome-wide protein concentrations in the cell. All the methods were applied to a sample from Escherichia coli chemostat culture. A Pearson squared correlation of approximately 0.6 among the three quantification methods was demonstrated. Importantly, the sum of quantified proteins by iBAQ and emPAI corresponded with the Lowry total protein quantification, demonstrating applicability of label-free methods for an accurate calculation of protein concentrations at the proteome level. The iBAQ method showed the best correlation between biological replicates, a normal distribution among all protein abundances, and the lowest variation among ribosomal protein abundances, which are expected to have equal amounts. Absolute quantitative proteome data enabled us to evaluate metabolic cost for protein synthesis and apparent catalytic activities of enzymes by integration with flux analysis. All the methods demonstrated similar ATP costs for protein synthesis for different cellular processes and that costs for expressing biomass synthesis related proteins were higher than those for energy generation. Importantly, catalytic activities of energy metabolism enzymes were an order or two higher than those of monomer synthesis. Interestingly, a staircase-like protein expression was demonstrated for most of the transcription units.