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(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.
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(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.
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hydrolysable tannin ht powder  (Kremer Pigments)
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(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.
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hydrolysate benson calibration standard h  (Eppendorf AG)
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(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.
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(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.
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(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.
Amino Acid Standard Mixtures, supplied by Pickering Laboratories, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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(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.

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