Bioactive Peptides from Tempeh Using Peptidecutter’s Cleavage

Abstract

empeh is an Indonesian traditional fermented food with rich nutrition and bioactive components. Rhizopus sp,especially Rhizopus oligosporus), lactic acid bacteria (Lactobacillus sp.), and yeast aremicroorganisms involved in Tempeh fermentation. An interesting offer of Bioinformatics (in silico method) as a supporting tool in molecular biology studies has emerged, such as in protein cleavage. This study utilized PeptideCutter application on ExPASyBioinformatics portal (https://web.expasy.org/peptide_cutter/) to cleave soy proteins glycinin G1, G2, G3, G4,G5,-conglycinin-chain,andchainusingavailable enzymes in the applicationwith twosimulations. Simulation I was conducted using enzyme complex produced by Lactobacillus sp.and Rhizopus oligosporus, whilesimulation II was used enzyme complex produced by Lactobacillus sp., Rhizopus oligosporus, and Klebsiella pneumonia. Simulation I was conducted using enzyme complex produced by Lactobacillus sp. and Rhizopus oligosporus, whilesimulation II was used enzyme complex produced by Lactobacillus sp., Rhizopus oligosporus, and Klebsiella pneumoniae. A total of 58 peptides was found from the simulation I and higher than simulation I (41 peptides). The bioactive peptides by the cleavages using PeptideCuttertool were dominated with dipeptides and only three peptides were in the form of tripeptides, namely Leu-Leu-Phe(glycininG1), Val-Val-Phe(glycininG5), and Arg-His-Lys(-conglycinin-chain). Bioactive peptides with antihypertensive and antidiabetic properties were mostly found in this in silicomethod of soybean cleavage.