Low molecular weight peptides derived from sarcoplasmic proteins produced by an autochthonous starter culture in a beaker sausage model

•A peptidomic study was conducted to characterize sarcoplasmic proteolysis on a sausage model.•Small peptides derived from the action of endogenous and microbial enzymes were identified.•The selected starter culture contributed to the enrichment and diversity of peptides.•New peptides and target proteins were detected as a result of proteolysis.•The new peptides can be proposed as biomarkers related to this starter culture.

This study focuses on meat protein degradation by different starter cultures. Sausage models inoculated with Lactobacillus curvatus CRL705 and Staphylococcus vitulinus GV318 alone and as a mixture were incubated 10 days at 22 °C. Low molecular weight peptides (<3 kDa) derived from sarcoplasmic proteins were analyzed by a peptidomic approach. A diverse number of protein fragments were identified. The greatest peptides diversity was obtained when the mixed starter culture was present. Peptides mainly arose from myoglobin, creatine-kinase, glyceraldehyde-3-phosphate-dehydrogenase and fructose-biphosphate-aldolase (ALDOA). ALDOA hydrolysis was attributed to the mixed starter culture; the released peptides could act as biomarkers for a specific sausage technology.SignificanceThe selection of a specific autochthonous starter culture guarantees the hygiene and typicity of fermented sausages. The identification of new peptides as well as new target proteins by means of peptidomics represents a significant step toward the elucidation of the role of microorganisms in meat proteolysis. Moreover, these peptides may be further used as biomarkers capable to certify the use of the applied autochthonous starter culture described here.

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