Bogor, 16-01-2018       Indonesia Version

Anti-microbes, immune-stimulant and anti-inflammation are the solutions for animal health. The use of bio-active peptides is trending in solving animal health issues.

 The use of conventional anti-microbes and anti-inflammation causes detrimental residual or side effects. An alternative solution and becoming popular in many countries is the use of bio-active peptides. The advantage of using bio-active peptides is that one peptide can have double functions so that the use of different medicines at the same time can be avoided. The use of bio-active peptides has been claimed as neutraceutical for future poultry production. Various methods can be used to produce bio-active peptides, and one of them is bio-active peptides as results of enzyme hydrolysis.

Protease enzyme is protein-degrading enzyme which can be used to produce bio-active peptides useful for improving animal health. Protease can be produced, among others, by microorganism.

Rhizopus oligosporus used in this study was from the collection of IRCVS Culture Collection  (BCC)  and  has  been  known  that they could be used to reduce B1 aflatoxin infeed, reduce B1 and M1 aflatoxin residue in duck meat, and had good viability when mixed in feed. Protease produced by R. oligosporus was used to produce bio-active peptides from soybean protein.

The Bacillus sp used in this study was found in horse milk in Bogor and had been known to have high protease activity and could hydrolyze protein of goat milk and dairy milk to produce peptides with high anti-microbes and anti-inflammation activities. Before producing anti-microbes and anti-inflammation peptides, the protease enzymes from R.oligosporus and Bacillus sp. were characterized in order to obtain the optimum condition for protein hydrolysis.

The growth condition most suitable for producing protease from R. Oligosporus was fish collagen substrate at pH 7 incubated for 5 days, or casein substrate incubated at pH 9 for 5 days. For producing protease from Bacillus sp, the optimum condition was casein substrate at pH 7 and incubated for 24 hours. Characterization of protease from R.oligosporus using HPLC and TLC 2 dimension showed that protease was composed of hydrophilic compounds, and hydrolysis had been done to protein of goat milk and horse milk using protease from R.oligosporus and Bacillus sp.; and test on the activity of hydrolysate to Candida albicans.