Abstract
New approaches to rapid examination of proteins and peptides in complex food matrices are of great interest to the community of food scientists. The aim of the study is to examine the influence of microwave irradiation on the acceleration of enzymatic cleavage and enzymatic digestion of denatured proteins in cooked meat of five species (cattle, horse, pig, chicken and turkey) and processed meat products (coarsely minced, smoked, cooked and semi-dried sausages). Severe protein aggregation occurred not only in heated meat under harsh treatment at 190 °C but also in processed meat products. All the protein aggregates were thoroughly hydrolyzed after 1 h of trypsin treatment with short exposure times of 40 and 20 s to microwave irradiation at 138 and 303 W. There were much more missed cleavage sites observed in all microwave-assisted digestions. Despite the incompleteness of microwave-assisted digestion, six unique peptide markers were detected, which allowed unambiguous identification of processed meat derived from the examined species. Although the microwave-assisted tryptic digestion can serve as a tool for rapid and high-throughput protein identification, great caution and pre-evaluation of individual samples is recommended in protein quantitation.
Highlights
Mass spectrometry-based proteomics has become an increasingly popular area of research in food science studies on protein interactions, identification and quantification
Despite the incompleteness of microwave-assisted digestion, six unique peptide markers were detected, which allowed unambiguous identification of processed meat derived from the examined species
This study examined the applicability of the microwave-assisted tryptic digestion for rapid and efficient recovery of peptide markers from industrially processed meat products
Summary
Mass spectrometry-based proteomics has become an increasingly popular area of research in food science studies on protein interactions, identification and quantification. The application of microspin columns, ultrasonic, infrared, microwave energy, high pressure or microreactors substantially reduced the sample preparation time, involving the steps of protein solubilization, reduction, alkylation, and digestion. The drawback of these new methods is that some instruments are expensive when commercially available, for instance powerful ultrasonic baths or microreactors. These new methods have been successfully implemented for protein analysis of simple mixtures and whole proteomes, but they have not been widely tested on processed food
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