bacto casitone  (Bacto Laboratories)

Journal: bioRxiv

Article Title: Catalytic Bacterial Nanocellulose Composite That Captures and Degrades PET Microplastics

doi: 10.64898/2026.06.05.730390

Figure Lengend Snippet: (a) Plot of absorbance at 280 nm as a function of temperature for a solution of enzyme (0.45 μM) in 50 mM glycine buffer (Gly-OH), pH 9.2. Data were normalized to offset differences in absorbances resulting from differing amino acid composition. The temperature ramp rate was 1°C/min. Quantitative assessment of the concentration of (b) TPA as measured by LC-MS, (c) total soluble aromatic products as measured by absorbance at 242 nm, at 20 °C, 40 °C, and 60 °C. Individual data points from 3 independent replicates shown with average (bar) and standard deviation (error bars). (d) The production of soluble aromatic products was continuously monitored by absorbance measurement at 242 nm over 300 min for both the CBD-PETase fusion and HotPETase at 60 °C. Graphs (b), (c) and (d) were generated from experiments using 0.45 μM enzyme and 2 g L -1 of μPET in Gly-OH (pH 9.2). All line graphs correspond to the average of n = 2, except for CBD-PETase in graph (d), where n = 3 for accurate representation of the lag-phase claim. Shaded regions of all line graphs represent the standard deviation.

Article Snippet: For E. coli expression of recombinant enzymes, 2× YT was prepared using 16 g L−1 casein hydrolysate (Thermo Scientific, AAJ12855P5), 10 g L−1 yeast extract (Thermo-Fisher Scientific, J23547.A1), and 5 g L−1 NaCl (Fisher Scientific, S271-3).

Techniques: Concentration Assay, Liquid Chromatography with Mass Spectroscopy, Standard Deviation, Generated

Journal: International Journal of Molecular Sciences

Article Title: Influence of Peptide-Rich Nitrogen Sources on GAD System Activation and GABA Production in Levilactobacillus brevis CRL 2013

doi: 10.3390/ijms27010082

Figure Lengend Snippet: Growth medium acidification ( A ) and GABA production ( B ) by Lv. brevis CRL 2013 in CDM or CDMg supplemented with different nitrogen sources. CDMg, chemically defined medium containing monosodium glutamate; CDMYE, CDM without glutamate supplemented with 1% yeast extract; CDMgYE, CDMg supplemented with 1% yeast extract; CDM Casitone 2%, CDM without glutamate supplemented with 2% Casitone; CDMgC0.5, CDMg supplemented with 0.5% Casitone; CDMgC, CDMg supplemented with 1%; CDMgC2, CDMg supplemented with 2% Casitone; CDMgC5, CDMg supplemented with 5% Casitone; CDMgVP, CDMg supplemented with 1% vegetable peptone. The pH profile observed in CDMgC0.5 was similar to those obtained in CDMg supplemented with 1% tryptone and 1% casamino acids, none of which supported detectable GABA production. Data are expressed as means ± SD from at least three independent biological replicates.

Article Snippet: To evaluate the role of nitrogen sources on GABA production, CDM containing 5% ( w / v ) monosodium glutamate (CDMg) as precursor was supplemented with different nitrogen sources ( ); 1% ( w / v ) yeast extract (Difco Laboratories, Sparks, MD, USA, CDMgYE), Casitone (Difco, 0.5, 1, 2, or 5% w / v ; CDMgC0.5, CDMgC, CDMC2 and CDMC5, respectively), Casamino Acids (Difco 1% w / v ; CDMgCA), Tryptone (Difco, 1% w / v ; CDMgT), or vegetable peptone (Difco, 1% w / v ; CDMgVP).

Techniques:

Journal: International Journal of Molecular Sciences

Article Title: Influence of Peptide-Rich Nitrogen Sources on GAD System Activation and GABA Production in Levilactobacillus brevis CRL 2013

doi: 10.3390/ijms27010082

Figure Lengend Snippet: Differential expression of shared proteins between CDMgYE and CDMgC relative to CDMg. From the 55 proteins overexpressed in both CDMgYE and CDMgC relative to CDMg, the 20 most strongly upregulated in CDMgYE were selected (left blue panel). Their corresponding expression levels in Casitone (CDMgC) are shown for comparison (right green panel). Proteins are ranked according to their mean expression differences (log2) in CDMgYE. The most overexpressed was GadB ( Q03U69 , glutamate decarboxylase), directly involved in GABA synthesis. Bars represent mean log2 expression differences from three independent biological replicates.

Article Snippet: To evaluate the role of nitrogen sources on GABA production, CDM containing 5% ( w / v ) monosodium glutamate (CDMg) as precursor was supplemented with different nitrogen sources ( ); 1% ( w / v ) yeast extract (Difco Laboratories, Sparks, MD, USA, CDMgYE), Casitone (Difco, 0.5, 1, 2, or 5% w / v ; CDMgC0.5, CDMgC, CDMC2 and CDMC5, respectively), Casamino Acids (Difco 1% w / v ; CDMgCA), Tryptone (Difco, 1% w / v ; CDMgT), or vegetable peptone (Difco, 1% w / v ; CDMgVP).

Techniques: Quantitative Proteomics, Expressing, Comparison