Enzyme Digestion
Enzymatic cleavage of complex protein structures into smaller peptide fragments enables detailed mass spectrometry analysis of structural proteins. Characterization of animal fibres like alpaca and cashmere relies on bottom up proteomics to identify species-specific peptide sequences. Trypsin breaks down extracted keratin into manageable fragments carrying predictable terminal residues.
Scope remains limited to soluble peptides generated after reductive alkylation and enzymatic digestion of raw or processed materials.
Peptide Separation
Reverse-phase liquid chromatography separates generated peptides by hydrophobic affinity prior to mass analysis. High-resolution mass spectrometers executing bottom up proteomics measure exact mass-to-charge ratios of eluting fragments. Tandem fragment spectra reveal amino acid order across distinct peptide chains.
Hydrophobic peptides elute late in the organic solvent gradient during liquid chromatography runs.
Sequence Mapping
Database matching algorithms compare measured fragment spectra against known genomic libraries. Applying bottom up proteomics allows laboratories to detect minor adulteration of luxury Cashmere yarns with domestic sheep wool. Biomarker peptides contain single amino acid substitutions that distinguish closely related animal species.
Chemical modifications like deamidation alter precursor masses and require targeted search parameters.
Fibre Identification
Mass spectral data provide unambiguous proof of origin for trade compliance checks. Reliable bottom up proteomics testing prevents mislabeled synthetic and natural fibre shipments from entering supply chains. Reproducible peptide spectra confirm raw material authenticity across processing batches.
Clear spectral matches resolve disputes between fibre suppliers and textile mills.