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The techniques of agriculture and animal husbandry at Tell Humeida, a Middle Uruk Period (Late Chalcolithic) site on the middle Syrian Euphrates, were studied using stable isotopes of bone collagen of domestic and wild mammals and from cereal and ruderal plant seeds. Two archaeological campaigns in 2009 and 2011 yielded a small collection of bones, most of which were taxonomically indeterminable. The work had to be interrupted due to the political conflict. The faunal study comprised collagen peptide fingerprinting for taxonomic identification, followed by isotopic analysis. Multiple 14C dating were performed to date the infill to around 3600 cal BC. An isotopic analysis of the sparse plant remains suggested that irrigation and manuring were common practices. Sheep and equids predominated in the faunal assemblage. Sheep grazed on manured soils, and their diet could include millet or another C4 plant, of which, however, no carpological remains were found. The diet of equids differed from that of sheep but also that of other wild ungulates (cervids/gazelles). Their isotopic signatures indicated that they grazed in humid areas, near the watercourse. These finds indicated a settlement that was closely linked to the availability of water, which made it possible to grow crops in an almost desert-like area, and the rearing of sheep. [ABSTRACT FROM AUTHOR]

The techniques of agriculture and animal husbandry at Tell Humeida, a Middle Uruk Period (Late Chalcolithic) site on the middle Syrian Euphrates, were studied using stable isotopes of bone collagen of domestic and wild mammals and from cereal and ruderal plant seeds. Two archaeological campaigns in 2009 and 2011 yielded a small collection of bones, most of which were taxonomically indeterminable. The work had to be interrupted due to the political conflict. The faunal study comprised collagen peptide fingerprinting for taxonomic identification, followed by isotopic analysis. Multiple 14C dating were performed to date the infill to around 3600 cal BC. An isotopic analysis of the sparse plant remains suggested that irrigation and manuring were common practices. Sheep and equids predominated in the faunal assemblage. Sheep grazed on manured soils, and their diet could include millet or another C4 plant, of which, however, no carpological remains were found. The diet of equids differed from that of sheep but also that of other wild ungulates (cervids/gazelles). Their isotopic signatures indicated that they grazed in humid areas, near the watercourse. These finds indicated a settlement that was closely linked to the availability of water, which made it possible to grow crops in an almost desert-like area, and the rearing of sheep.

Proteomic methods and approaches to the detection of tissue-specific and tissue-generating proteins and peptides – which form corrective properties – in studied meat samples and specially developed meat products were successfully tried out in 2016–2017. The methods allow one to confirm protein and peptide authenticity and also detect bio-markers of proteolytic changes in meat after slaughter. The following proteomic techniques were used in the present research: two-dimensional O’Farrell electrophoresis with isoelectrofocusing in ampholin and immobilin pH gradients, the detection of proteins on two-dimensional electrophoregrams by staining with Coomassie R-250 and silver nitrate, and mass spectrometric identification of proteins by means of MALDI-TOF and MS/MS methods. Contractile actomyosin complex proteins, such as myosin light chains and tropomyosins, were the most informative among proteins of species specificity. It is also necessary to mention that earlier experiments allowed us to choose enzymes which play a part in carbohydrate metabolism (glyceraldehyde 3-phosphate dehydrogenase and β-enolase) as markers. In addition to the listed proteins, myoglobins, actins, and several other proteins in horse meat have showed high species specificity and have been detected well. A system of species specificity (authenticity) of meat raw materials was suggested. The system allows the presence of pork, beef, horse, and camel meat to be detected in both raw and heat-treated products if the content is 5% and more. The data has been obtained by means of bioinformatics, а highly useful tool for formulating an algorithm to identify the protein markers for the Atlas “Proteomic profiles of farm animals meat proteins”. “Proteomic profiles of farm animals muscle proteins”.

The aim of this study is to explore differences in the peptidomics of Saccharomyces pastorianus protein hydrolysates treated with different enzymes. Briefly, differences in the peptide fingerprints and active peptides of neutral protease/papain-hydrolyzed S. pastorianus were analyzed using ultra-high performance liquid chromatography-high resolution mass spectrometry (UHPLC-HRMS) combined with PEAKS Online 1.7 analysis software, Peptide Ranker, and the BIOPEP database. Compared to traditional databases, the PEAKS Online uses de novo sequencing for analysis to obtain oligopeptides smaller than pentapeptides. It provides more comprehensive data of the peptide sample. In this study, enzymatic hydrolysates of S. pastorianus protein were prepared under the optimum conditions of neutral protease and papain respectively. In total, 7221 and 7062 polypeptides were identified in the hydrolysates of neutral protease and papain, respectively; among these polypeptides, 980 were common to the two enzymes. The 6241 and 6082 unique peptides found in the hydrolysates of neutral protease and papain, respectively, indicated that the peptide fingerprints of the two hydrolysates are quite different. Peptide Ranker predicted that 3013 (41.73%) and 3095 (43.83%) peptides were potentially bioactive in the hydrolysates of neutral protease and papain, respectively. According to the BIOPEP database, neutral protease and papain contained 295 and 357 active peptides, respectively; these peptides were mainly composed of angiotensin converting enzyme (ACE) inhibitors and dipeptidyl peptidase IV inhibitors and antioxidant peptides. The number of active peptides in the hydrolysate of papain was higher than that in the hydrolysate of neutral protease, but the total ion intensity of active peptides in the former was lower than that in the latter. This study revealed the influence of protease type on the composition of enzymatic hydrolysates from S. pastorianus protein. The above results provide a reference for the development of functional products of S. pastorianus protein peptides and the high-value utilization of yeast resources.