Effects of fermentation and enzymatic treatment on phenolic compounds and soluble proteins in oil press cakes of canola (Brassica napus).

To develop novel processes for valorizing agro-industry side-streams, canola (Brassica napus) oil press cakes (CPC) were treated with lactic acid bacteria, carbohydrase, and protease. Altogether 29 protein-rich liquid fractions were obtained, of which the composition was analyzed using chromatographic and mass spectrometric methods. A clear association was revealed between the treatments and phenolic profile.

Impact of enzymatic pre-treatment on composition of nutrients and phytochemicals of canola (Brassica napus) oil press residues.

The study aimed to develop a biorefining process to recover proteins and dietary fibres from a food industry side-stream, canola (Brassica napus) oil pressing residues. The materials were treated with commercial protease, carbohydrase, and phytase to obtain protein-rich supernatants and fibre-rich precipitates. The compositions of these fractions were analyzed using LC-MS (glucosinolates and phenolics) and GC-MS (sugars, acids, and amino acids).

Impact of Fermentation and Phytase Treatment of Pea-Oat Protein Blend on Physicochemical, Sensory, and Nutritional Properties of Extruded Meat Analogs.

Plant materials that are used for the production of extruded meat analogs are often nutritionally incomplete and also contain antinutrients, thus there is a need to explore alternative plant proteins and pre-treatments. This study demonstrates application of phytase and fermentation to a pea-oat protein blend with a good essential amino acid profile and subsequent texturization using extrusion cooking. Enzymatic treatment reduced the content of antinutrient phytic acid by 32%.

Inhibition of CREB phosphorylation by conjugates of adenosine analogues and arginine-rich peptides, inhibitors of PKA catalytic subunit.

Bisubstrate inhibitors of protein kinases associate simultaneously with two substrate-binding sites of the kinase and thus potentially possess better inhibitory potency and selectivity than inhibitors binding to only the conserved ATP-site of the kinase. We have previously used conjugates of adenosine analogues and arginine-rich peptides (ARCs) to develop proteolytically stable cell plasma membrane-permeable bisubstrate inhibitors whose biochemical affinities towards several basophilic protein kinases of the AGC group are in the picomolar range. The potency of bisubstrate inhibitors to affect the phosphorylation of proteins in living cells has been described in a limited number of publications.

Protein-induced long lifetime luminescence of nonmetal probes.

Time-resolved luminometry-based assays have great potential for measurements in complicated biological solutions and living cells as the measured signal can be easily distinguished from nanosecond lifetime background fluorescence of organic compounds and autofluorescence of cells. In the present study we discovered that binding of a thiophene- or a selenophene-containing heteroaromatic moiety (luminescence donor) to the purine-binding pocket of a protein kinase (PK) induces long lifetime photoluminescence signal that is largely intensified through efficient energy transfer to a fluorescent dye present in close proximity to the luminescence donor. The developed ARC-Lum probes possessing 19-266 μs luminescence lifetime when associated with the target kinase can be used for determination of activity of basophilic PKs, characterization of inhibitors of PKs, and as cAMP sensors.

Effect of the structure of adenosine mimic of bisubstrate-analog inhibitors on their activity towards basophilic protein kinases.

Previously reported structural fragments that associate with the ATP-binding pocket of basophilic protein kinases were conjugated with d-arginine-containing peptides. Inhibitory potency of the resulting bisubstrate-analog inhibitors towards PKA and ROCK-II extended to subnanomolar range. The conjugates incorporating 2-pyrimidyl-5-amidothiophene fragment had the highest activity and at 100 nM concentration exhibited over 80% inhibition of most of the tested basophilic kinases of the AGC group.