Feather protein lysate optimization and feather meal formation using YNDH protease with keratinolytic activity afterward enzyme partial purification and characterization

Abstract Incubation parameters used for the creation of a protein lysate from enzymatically degraded waste feathers using crude keratinase produced by Laceyella sacchari strain YNDH were optimized Response Surface Methodology (RSM); amino acids quantification was also estimated. The optimization elevated total to 2089.5 µg/ml through application following optimal conditions: time 20.2 h, feather concentration (conc.) 3 g%, activity 24.5 U/100 ml, pH 10, and cultivation temperature 50 °C. Feather Protein Lysate (FPL) found be enriched with essential rare acids. Additionally, this enzyme group partially purified, some its characteristics studied. Crude enzymes first concentrated an Amicon Ultra 10-k centrifugal filter, then proteins applied "Q FF" strong anion column chromatography. purified has estimated molecular masses ranging 6 10 kDa. maximum observed at 70 °C 10.4. Most protease/keratinase nearly same when measured both casein keratin-azure as substrates, suggesting that these three bands work together in order degrade keratin macromolecule. Interestingly, keratinolytic not inhibited ethylenediamine tetraacetic acid (EDTA), phenylmethanesulfonyl fluoride (PMSF), or iron-caused activation, indicating presence mixed serine – metallo type.