{"database":"MassIVE","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["ftp://massive-ftp.ucsd.edu/v08/MSV000095524/"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Anton Stepnov"],"instrument_platform":["RSLCnano UHPLC/Q-Exactive"],"species":["Galleria Mellonella (ncbitaxon:7137)"],"full_dataset_link":["https://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=517336e6127a466592dba48ce4d93290"],"submitter_email":["anton.stepnov@nmbu.no"],"submitter_affiliation":["NMBU"],"sample_protocol":[""],"repository":["MassIVE"],"file_size":["2"],"ptm_modification":["carbamidomethyl cysteine"],"data_protocol":[""],"pubmed_abstract":["Biocatalytic degradation of non-hydrolyzable plastics is a rapidly growing field of research, driven by the global accumulation of waste. Enzymes capable of cleaving the carbon-carbon bonds in synthetic polymers are highly sought-after as they may provide tools for environmentally friendly plastic recycling. Despite some reports of oxidative enzymes acting on non-hydrolyzable plastics, including polyethylene or poly(vinyl chloride), the notion that these materials are susceptible to efficient enzymatic degradation remains controversial, partly driven by a general lack of studies independently reproducing previous observations. Here, we attempt to replicate two recent studies reporting that deconstruction of polyethylene and poly(vinyl chloride) can be achieved using an insect hexamerin from Galleria mellonella (so-called \"Ceres\") or a bacterial catalase-peroxidase from Klebsiella sp., respectively. Reproducing previously described experiments, we do not observe any activity on plastics using multiple reaction conditions and multiple substrate types. Digging deeper into the discrepancies between the previous data and our observations, we show how and why the original experimental results may have been misinterpreted."],"pubmed_title":["Revisiting the activity of two poly(vinyl chloride)- and polyethylene-degrading enzymes."],"pubmed_authors":["Stepnov Anton A AA, Lopez-Tavera Esteban E, Klauer Ross R, Lincoln Clarissa L CL, Chowreddy Ravindra R RR, Beckham Gregg T GT, Eijsink Vincent G H VGH, Solomon Kevin K, Blenner Mark M, Vaaje-Kolstad Gustav G"],"pubmed_title_synonyms":["Low-Density Polyethylene, Polyethylene, Enzyme, Low Density Polyethylene, Activity, Low-Density, enzymes, High-Density, Biocatalysts, LDPE, Polythene, HDPE, homopolymer, Ethene, High-Density Polyethylene, Biocatalyst., High Density Polyethylene, enzyme activity, General activity"],"description_synonyms":["liquid chromatography tandem mass spectroscopy, LC-MS2, Raw., Svc, Bru, LCMSMS, Col4a-1, determination, protein complex, Proteins, LC-MS/MS, Gene, proteins, protein, protein-containing complex, LC-MS-MS, Protein Gene Products, Gene Proteins, protein polypeptide chains, LC/MS/MS, native protein, natural protein, polypeptide chain, liquid chromatography-tandem mass spectroscopy, LC-MSMS, chemical analysis, Protein, Gene Products, liquid chromatography tandem mass spectrometry, assay, Del(8)44H, protein aggregate"],"pubmed_abstract_synonyms":["biochemical pathways, macromolecules, single-organism catabolic process, multicellular organismal catabolic process, Low-Density Polyethylene, artificial sequence, who., Activity, Laboratory, Biocatalysts, P62, dSmurf1, High Density Polyethylene, carbon, Progress Reports, sci, cellular catabolism, organ field, DSmurf, Investigative, Carbon-12, Summary Report, HOW, How, cellular degradation, field, Research Activity, synthetic genetic interaction (sensu inequality), Laboratory Research, Summary Reports, l(3)j5D5, Priorities, 24B, C, l(3)s2612, enzymes, Plastic, Progress Report, breakdown of chemical, Research, catabolism, developmental field, LDPE, Polythene, homopolymer, stru, synthetic genetic interaction defined by inequality, Phalaena mellonella, l(3)S053606, CG10293, Progress, l(3)j5B5, reaction, Kohlenstoff, Enzyme, Field Reports, d-smurf, Smurf, Carbon, DmelCG10293, biotransformation, Development and Research, Research Priority, Investigative Reports, CG4943, D-smurf, cellular breakdown, 0904/17, bacterial catalase-peroxidase, polymer molecule, degradation, clone 2.39, Ethene, Research Priorities, artificial gene, enzyme activity, future organ, synthetic DNA, Lack, qkr, Dsmurf, carbone, l(3)S090417, Donovania, carbono, Vitreous, Polyethylene, dSmurf, Priority, Investigative Report, SZ1, Smurf ubiquitin ligase, KH93F, Research Reports, Research Activities, synthetic, secretion, Insects, breakdown of molecule, Research and Development, polymer, breakdown, Low Density Polyethylene, KatA catalase peroxidase, biodegradation, Low-Density, High-Density, DmelCG4943, Legionella, 6C, katA protein, HDPE, Field, High-Density Polyethylene, Who/How, synthetic constructs, polymers, Calymmatobacterium, Insect, Carbon 12, Activities, breakdown of substance, Vitreous Carbon, SYNTHETIC CONSTRUCT sequences, Report, Polymer, Reports, carbonium, Biocatalyst, qkr[93F], artificial, anon-EST:Liang-2.39, Summary, macromolecule, General activity, Field Report, Hyalococcus"],"name_synonyms":["liquid chromatography tandem mass spectroscopy, LC-MS2, Gene., LCMSMS, determination, protein complex, Proteins, LC-MS/MS, proteins, protein, protein-containing complex, LC-MS-MS, Protein Gene Products, Gene Proteins, protein polypeptide chains, LC/MS/MS, native protein, natural protein, polypeptide chain, liquid chromatography-tandem mass spectroscopy, LC-MSMS, chemical analysis, Protein, Gene Products, liquid chromatography tandem mass spectrometry, assay, protein aggregate"],"additional_accession":[]},"is_claimable":false,"name":"LC-MS/MS analysis of the purified Ceres protein","description":"LC-MS/MS analysis of the purified recombinantly produced Ceres protein: raw spectrum file","dates":{"publication":"Tue Aug 06 03:53:00 BST 2024"},"accession":"MSV000095524","cross_references":{"pubmed":["39353919"]}}