Production and characterization of novel thermo- and organic solvent-stable keratinase and aminopeptidase from Pseudomonas aeruginosa 4-3 for effective poultry feather degradation

Feather biodegradation is an important premise for efficient resource development and utilization, in which keratinase plays an important role. However, there are few keratinases that combine the high activity, thermal stability, and organic solvent tolerance required for industrialization. This paper reported an efficient feather-degrading Pseudomonas aeruginosa 4-3 isolated from slaughterhouses. After 48 h of fermentation by P. aeruginosa 4-3 in a feather medium at 40 degrees C, pH 8.0, keratinase was efficiently produced (295.28 +/- 5.42 U/mL) with complete feather degradation (95.3 +/- 1.5%). Moreover, the keratinase from P. aeruginosa 4-3 showed high optimal temperature (55 degrees C), good thermal stability, wide pH tolerance, and excellent organic solvent resistance. In addition, P. aeruginosa 4-3-derived aminopeptidases also exhibit excellent thermal stability and organic solvent tolerance. Encouragingly, the reaction of crude keratinase and aminopeptidase with feathers for 8 h resulted in a 78% degradation rate of feathers. These properties make P. aeruginosa 4-3 keratinase and aminopeptidase ideal proteases for potential applications in keratin degradation, as well as provide ideas for the synergistic degradation of keratin by multiple enzymes.