Development and Evaluation of a Fermented Pistachio-Based Beverage Obtained by Colloidal Mill.

The aim of the present study was to develop a fermented pistachio beverage as a plant-based alternative to milk-based drinks. For this purpose, a colloidal mill was used to finely grind and homogenize the pistachios to obtain a homogeneous consistency and prevent sedimentation. In addition, lactic acid bacteria fermentation was used to develop unique flavours and characteristics in the final product and to achieve microbiological stability for up to 30 days of storage a 4 °C. The formulated beverages were evaluated for chemical-physical characteristics (pH, organic acid production, and fructose, sucrose, and glucose content), nutritional profile (proximate composition, amino acid and GABA content), and volatile organic composition by HS-SPME-GC/MS analysis. The pistachio-based beverages were characterized by a good source of protein, fat, fiber, and minerals (mainly K and P). The colloidal mill contributed to creating a homogeneous texture and to making the nutrients readily available to the starter microorganisms, which reached concentrations above 108 ufc/mL in the final products. The beverages were characterized by pronounced acidity and some by the presence of acetoin and 2,3-butanedione, volatile components associated with a yogurt- or kefir-like aroma. This innovative approach provides an alternative to traditional milk-based beverages and highlights the role of LAB in the development of nutritious and attractive plant-based beverages.

Isolation and identification of cholesterol esterase and pancreatic lipase inhibitory peptides from brewer's spent grain by consecutive chromatography and mass spectrometry.

The isolation and identification of cholesterol esterase (CE) and pancreatic lipase (PL) inhibitory peptides obtained from the protein hydrolysate of brewer's spent grain (BSG) was performed. BSG peptides were fractionated and purified sequentially by anion exchange, gel filtration (FPLC), and reversed phase high-performance liquid chromatography (RP-HPLC). The fractions obtained from each chromatographic step were collected and the in vitro enzyme inhibitory activity was evaluated. The chromatographic purification process increased the in vitro activities. The most active fractions were evaluated using MALDI-TOF tandem mass spectrometry, which identified three peptides: a peptide with the highest CE inhibition capacity (WNIHMEHQDLTTME) and two peptides with PL inhibition capacity (DFGIASF and LAAVEALSTNG). These three peptides showed hydrophobic and acidic amino acid residues (Asp and Glu) and/or their amines (Asn and Gln), which could be a common feature among lipid-lowering peptides related to CE and PL enzyme inhibition. The in silico studies showed that the three peptides had high hydrophobicity and were susceptible to enzymatic hydrolysis performed by trypsin, pepsin, and pancreatin. The BSG byproduct was a good source of CE and PL inhibitory peptides, thus adding value to this byproduct of the beer industry. This is the first report to demonstrate that BSG peptides can inhibit CE and PL enzymes.