Antioxidant and Antimicrobial Potential of Peptide from Rabbit Meat Hydrolysate Prepared by Trypsin and Zingibain.

Abstract

<b>Background and Objective:</b> Rabbit meat is a livestock product potentially viable as a protein source to obtain peptides. Antioxidant and antimicrobial peptides are ingredients extracted from various foods through enzymatic hydrolysis, chemical hydrolysis and fermentation to produce health-promoting foods. This research aims to investigate the potential of rabbit meat as a source of antioxidant and antimicrobial peptides through hydrolysis using trypsin and zingibain enzymes. <b>Materials and Methods:</b> This research conducted an explorative-descriptive approach, focusing on antioxidant and antimicrobial activity. Rabbit meat was extracted using trypsin, zingibain and a combination of trypsin and crude extract zingibain. The hydrolyzed rabbit meat extract was tested at intervals of 0, 2, 6, 16, 24, 40 and 48 hrs to determine the degree of hydrolysis and the profile of hydrolyzed proteins with electrophoresis SDS PAGE. The antioxidant activity was tested using the DPPH method and the antimicrobial activity using agar well diffusion method. <b>Results:</b> The degree of hydrolysis increased with the hydrolysis time. The highest protein content of rabbit meat extract hydrolyzed with trypsin was 287.65 mg/mL, observed during 12 hrs hydrolysis. The optimum conditions for the hydrolysis of rabbit meat protein were obtained at 24 hrs, with an IC₅₀ value of 52.45% hydrolyzed by trypsin. As per antimicrobial activities, <i>Escherichia coli</i> and <i>Salmonella</i> sp. were more effective in inhibiting rabbit meat hydrolysates compared to <i>Pseudomonas aeruginosa</i> and <i>Staphylococcus aureus</i>. The inhibition of all pathogen increased until 12 hrs hydrolysis but decreased in 24 hrs hydrolysis. <b>Conclusion:</b> The combination zingibain enzyme and trypsin is feasible for hydrolyzing rabbit meat and the optimum hydrolysis time was 24 hrs with IC₅₀ 52.45 ppm, although accompanied by reduction in antibacterial activities.