| dc.description.abstract | Gelatin, a partial hydrolysis product of animal collagen has been widely used in Indonesia processing industry. The source of gelatin, however, is strictly regulated due to religious concern. Thus, the method that could differentiate the source of gelatin is needed. This research was aimed to predict biomarker peptides using bioinformatics approach that could be used to differentiate the source of gelatin by means of mass spectrometry. Collagen sequences from cattle, pigs, chickens, and fish were obtained from the UniProt database. The sequences were in silico digested using trypsin and chymotrypsin in PeptideMass software. The resulting peptides were filtered following the criteria for mass spectrometry. In general, trypsin digestion produced higher number of specific peptides compared to that of chymotrypsin enzyme. The number of peptide sequences resulting from hydrolysis with the chymotrypsin indicates the enzyme is less specific in cutting protein than the trypsin enzyme. Trypsin is more suitable for finding biomarkers than chymotrypsin. Some of the specific peptides detected can be used to differentiate the species from which gelatin is derived. | id |
