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Title

Identification of protein remnants in insoluble geopolymers using TMAH thermochemolysis/GC-MS

AuthorsKnicker, Heike ; Río Andrade, José Carlos del ; Hatcher, Patrick G.; Minard, Robert D.
KeywordsTMAH/thermochemolysis
Refractory organic nitrogen
GC/MS
Humin
Algae
Peptide
Amino acid
Protein
Issue Date2001
PublisherElsevier
CitationOrganic Geochemistry 32(3): 397-409 (2001)
AbstractThermochemolysis with tetramethylammonium hydroxide (TMAH) was utilized to analyze peptide-like material in insoluble residues of geochemical samples. Product identification was performed by gas chromatography/mass spectrometry using bovine albumin and di-, tri- and oligo-peptides. Most of the identified amino acid derivatives originate from the cleavage of the peptide bonds and subsequent methylation of the carboxylic and the amino groups. Some products are explained by deamination of aromatic amino acids. Only two products were identified that experienced chemical rearrangement after methylation. TMAH/thermochemolysis of algal material resulted in products comparable to those obtained from albumin. Amino acid derivatives were also identified among the TMAH/thermochemolysis products of refractory biopolymer of the alga Scenedesmus communis and the HCl-hydrolysis residue of the humin from an algal sapropel. These results strongly indicate that for those samples, hydrolysis fails to extract all proteinaceous and peptide-like components, possibly because these approaches rely on extraction of peptides and amino acids into solution and some of these are entrapped within a non-extractable hydrophobic network. However, alternative explanations for this behavior are possible. For example, at the higher temperatures and pressures and strongly basic conditions used in TMAH themochemolysis, penetration of this hydrophobic barrier takes place thus allowing breakdown and methylation of protein remnants.
Description13 páginas, 5 figuras, 2 tablas.
URIhttp://hdl.handle.net/10261/39869
ISSN0146-6380
Appears in Collections:(IRNAS) Artículos
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