Dataset Information

Comparing targeted and non-targeted high-resolution mass spectrometric approaches for assessing advanced oxidation reactor performance.

ABSTRACT: High resolution mass spectrometry (HR-MS) offers the opportunity to track large numbers of non-target analytes through water treatment processes, providing a more comprehensive view of reactor performance than targeted evaluation. Both approaches were used to evaluate the performance of a pilot scale advanced oxidation process (AOP) employing ultraviolet light and hydrogen peroxide (UV/H2O2) to treat municipal wastewater effluent. Twelve pharmaceuticals and personal care products were selected as target compounds and added to reactor influent. Target compound removal over a range of flow rates and hydrogen peroxide addition levels was assessed using a liquid chromatograph combined with a quadrupole time-of-flight mass spectrometer (LC-qTOF-MS). Target compound removals were used to determine hydroxyl radical concentrations and UV fluence under pilot scale conditions. The experiments were also analyzed using a nontarget approach, which identified "molecular features" in either reactor influent or effluent. Strong correlation (r = 0.94) was observed between target compound removals calculated using the targeted and non-targeted approaches across the range of reactor conditions tested. The two approaches also produced consistent rankings of the performance of the various reactor operating conditions, although the distribution of compound removal efficiencies was usually less favorable with the broader, nontarget approach. For example, in the UV only treatment 8.3% of target compounds and 2.2% of non-target compounds exhibited removals above 50%, while 100% of target compounds and 74% of non-target compounds exhibited removals above 50% in the best condition tested. These results suggest that HR-MS methods can provide more holistic evaluation of reactor performance, and may reduce biases caused by selection of a limited number of target compounds. HR-MS methods also offer insights into the composition of poorly removed compounds and the formation of transformation products, which were widely detected.

SUBMITTER: Parry E

PROVIDER: S-EPMC7108753 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Comparing targeted and non-targeted high-resolution mass spectrometric approaches for assessing advanced oxidation reactor performance.

Parry Emily E Young Thomas M TM

Water research 20160725

High resolution mass spectrometry (HR-MS) offers the opportunity to track large numbers of non-target analytes through water treatment processes, providing a more comprehensive view of reactor performance than targeted evaluation. Both approaches were used to evaluate the performance of a pilot scale advanced oxidation process (AOP) employing ultraviolet light and hydrogen peroxide (UV/H<sub>2</sub>O<sub>2</sub>) to treat municipal wastewater effluent. Twelve pharmaceuticals and personal care pr ...[more]

PMID: 27518144

Similar Datasets

Project description:Covalent labeling and mass spectrometry are seeing increased use together as a way to obtain insight into the 3-dimensional structure of proteins and protein complexes. Several amino acid specific (e.g., diethylpyrocarbonate) and non-specific (e.g., hydroxyl radicals) labeling reagents are available for this purpose. Diethylpyrocarbonate (DEPC) is a promising labeling reagent because it can potentially probe up to 30% of the residues in the average protein and gives only one reaction product, thereby facilitating mass spectrometric analysis. It was recently reported, though, that DEPC modifications are labile for some amino acids. Here, we show that label loss is more significant and widespread than previously thought, especially for Ser, Thr, Tyr, and His residues, when relatively long protein digestion times are used. Such label loss ultimately decreases the amount of protein structural information that is obtainable with this reagent. We find, however, that the number of DEPC modified residues and, thus, protein structural information, can be significantly increased by decreasing the time between the covalent labeling reaction and the mass spectrometric analysis. This is most effectively accomplished using short (e.g., 2 h) proteolytic digestions with enzymes such as immobilized chymotrypsin or Glu-C rather than using methods (e.g., microwave or ultrasonic irradiation) that accelerate proteolysis in other ways. Using short digestion times, we show that the percentage of solvent accessible residues that can be modified by DEPC increases from 44% to 67% for cytochrome c, 35% to 81% for myoglobin, and 76% to 95% for ?-2-microglobulin. In effect, these increased numbers of modified residues improve the protein structural resolution available from this covalent labeling method. Compared with typical overnight digestion conditions, the short digestion times decrease the average distance between modified residues from 11 to 7 Å for myoglobin, 13 to 10 Å for cytochrome c, and 9 to 8 Å for ?-2-microglobulin.

Dataset Information

Comparing targeted and non-targeted high-resolution mass spectrometric approaches for assessing advanced oxidation reactor performance.

Publications

Comparing targeted and non-targeted high-resolution mass spectrometric approaches for assessing advanced oxidation reactor performance.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets