Enzymatic activity and amino acid production by indigenous keratinolytic strains on the various poultry feather substrate

Abstract This study aims to evaluate the capability of extracellular protease hydrolyze keratin substrates local poultry feathers and observing amino acid profile. The indigenous strains ( Bacillus cereus TD5B, LS2B, Pseudomonas sp. PK4) were used in this study, obtained data analysed descriptively. TD5B has a maximum activity at 0.003849062 unit/ml 0.000310042 on casein commercial substrates. Each hydrolyzed consisted Aspartic Acid, Glutamic Serine, Glycine, Valine, Phenylalanine, Ileucine, Leucine, Lysine. differences between three feather meals acid’s concentration, specific (Threonine) kampung chicken meals, Alanine layer also goose meals. SDS-PAGE results showed that molecular weight keratinase was observed 100 kDa. In highest substrate degradation by (21.25%). During 21 days, LS2B could 38.8% during 23 PK4 39.8% for 24 days.