TY - JOUR
T1 - Wet degradation of keratin proteins
T2 - Linking amino acid, elemental and isotopic composition
AU - Von Holstein, I. C.C.
AU - Penkman, K. E.H.
AU - Peacock, E. E.
AU - Collins, M. J.
PY - 2014/10/15
Y1 - 2014/10/15
N2 - Rationale Archaeological keratin samples are increasingly the subject of palaeodietary, provenancing and dating studies. Keratin samples from wet archaeological contexts are microbiologically and chemically degraded, causing differential diagenesis of protein structures in hair fibres. The effects of these processes on the analytical parameters of interest are currently unknown. METHODS This study examined the impact of degradation of wool fibres on isotopic (δ13C, δ15N, un-exchangeable δ2H and δ18O values) composition. It compared two models of archaeological protein degradation in wet burial environments: (1) short term (up to 8-years) experimental burial in three contrasting soil environments; and (2) laboratory wet conditions, in which elevated temperature (80-°C, 110-°C, and 140-°C) and pressure simulated longer exposure. Elemental and amino acid (AA) composition were also measured. RESULTS In experimentally soil-buried samples, AA, elemental and isotopic composition changes were small, despite extensive macroscopic alteration. Isothermally heated samples showed preferential loss of hydrophilic AAs (Asx, Glx, Ser, Gly) from wool residues, with depletion in 2H and 18O at higher temperatures (up to -73‰ change in δ2H and -2.6‰ in δ18O values). The δ13C and δ15N values showed little change except in densely pigmented samples at low temperatures only. Samples dyed with madder/alum were better preserved than undyed samples. CONCLUSIONS Diagenesis in experimentally soil-buried wool textiles was consistent with microbiological, non-protein-selective activity, in contrast to highly AA-selective hydrolytic behaviour under laboratory wet conditions. Changes in δ2H and δ18O values were correlated with degree of AA change, but the δ13C and δ15N values were not. The results contribute to a baseline for interpreting analytical data from archaeological hair samples preserved by burial in wet environments.
AB - Rationale Archaeological keratin samples are increasingly the subject of palaeodietary, provenancing and dating studies. Keratin samples from wet archaeological contexts are microbiologically and chemically degraded, causing differential diagenesis of protein structures in hair fibres. The effects of these processes on the analytical parameters of interest are currently unknown. METHODS This study examined the impact of degradation of wool fibres on isotopic (δ13C, δ15N, un-exchangeable δ2H and δ18O values) composition. It compared two models of archaeological protein degradation in wet burial environments: (1) short term (up to 8-years) experimental burial in three contrasting soil environments; and (2) laboratory wet conditions, in which elevated temperature (80-°C, 110-°C, and 140-°C) and pressure simulated longer exposure. Elemental and amino acid (AA) composition were also measured. RESULTS In experimentally soil-buried samples, AA, elemental and isotopic composition changes were small, despite extensive macroscopic alteration. Isothermally heated samples showed preferential loss of hydrophilic AAs (Asx, Glx, Ser, Gly) from wool residues, with depletion in 2H and 18O at higher temperatures (up to -73‰ change in δ2H and -2.6‰ in δ18O values). The δ13C and δ15N values showed little change except in densely pigmented samples at low temperatures only. Samples dyed with madder/alum were better preserved than undyed samples. CONCLUSIONS Diagenesis in experimentally soil-buried wool textiles was consistent with microbiological, non-protein-selective activity, in contrast to highly AA-selective hydrolytic behaviour under laboratory wet conditions. Changes in δ2H and δ18O values were correlated with degree of AA change, but the δ13C and δ15N values were not. The results contribute to a baseline for interpreting analytical data from archaeological hair samples preserved by burial in wet environments.
UR - http://www.scopus.com/inward/record.url?scp=84906666035&partnerID=8YFLogxK
U2 - 10.1002/rcm.6999
DO - 10.1002/rcm.6999
M3 - Journal article
C2 - 25156602
AN - SCOPUS:84906666035
SN - 0951-4198
VL - 28
SP - 2121
EP - 2133
JO - Rapid Communications in Mass Spectrometry
JF - Rapid Communications in Mass Spectrometry
IS - 19
ER -