Enhanced keratinase production by Bacillus subtilis amr using experimental optimization tools to obtain feather protein lysate for industrial applications

• Published in: 3 Biotech 2022-04, Vol.12 (4), p.90-90, Article 90
• Main Authors: Mazotto, Ana Maria, Cedrola, Sabrina M. L., de Souza, Edilma P., Couri, Sonia, Vermelho, Alane B.
• Format: Article
• Language: English
• Subjects: Agriculture; Ammonium sulfate; Bacillus subtilis; Biodegradation; Bioinformatics; Biomaterials; Biotechnology; Calcium ions; Cancer Research; Chemistry; Chemistry and Materials Science; Copper; Degradation; Enzymatic activity; Feathers; Fermentation; Hydrolysates; Industrial applications; Information processing; Inoculum; Keratinase; Keratinocytes; Magnesium; Nitrogen sources; Optimization; Original; Original Article; Proteins; Stem Cells; Sucrose
• ISSN: 2190-572X; 2190-5738
• DOI: 10.1007/s13205-022-03153-y

The poultry industry produces millions of tons of feathers waste that can be transformed into valuable products through bioprocess. The study describes the enhanced keratinase and feather hydrolysate production by Bacillus subtilis AMR. The metabolism of each microorganism is unique, so optimization tools are essential to determine the best fermentation parameters to obtain the best process performance. The evaluation of different propagation media indicated the constitutive production of two keratinases of approximately 80 kDa. The combination of Mn 2+ , Ca 2+ , and Mg 2+ at 0.5 mM improved the keratinolytic activity and feather degradation 1.5-fold, while Cu 2+ inhibited the enzymatic activity completely. Replace yeast extract for sucrose increased the feather hydrolysate production three times. The best feather concentration for hydrolysate production was 1.5% with an inoculum of 10 8  CFU/mL and incubation at 30 °C. None of the inorganic additional nitrogen sources tested increased hydrolysate production, although (NH 4 ) 2 SO 4 and KNO 3 improved enzymatic activity. The optimization process improved keratinolytic activity from 205.4 to 418.7 U/mL, the protein concentration reached 10.1 mg/mL from an initial concentration of 3.9 mg/mL, and the feather degradation improved from 70 to 96%. This study characterized keratinase and feather hydrolysate production conditions offering valuable information for exploring and utilizing AMR keratinolytic strain for feather valorization.