Enzymatic bioconversion of feather waste with keratinases of Bacillus cereus PCM 2849

Enzymatic preparation from culture of keratinolytic Bacillus cereus PCM 2849 was applied for hydrolysis of whole chicken feathers, after sulphitolytic pretreatment. This process was optimized using a three-factor Box-Behnken design, where the effect of substrate concentration, sulphite concentration during pretreatment and reaction temperature was evaluated on the release of amino acids. Obtained results revealed the highest impact of reaction temperature, followed by substrate content and sulphite during pretreatment. Optimal process conditions were established, i.e. temperature 44.4°C, feathers 4.7% and treatment with 25.3 mM sulphite. Amino acid composition of the obtained hydrolysate was analyzed. Glutamic acid (9.21 g·kg⁻¹) and proline were dominant, however significant amount of branched-chain amino acids was also observed. The FTIR analysis of residual substrate revealed the cleavage of disulphide bonds in keratin through the presence of thioester residues. The absence of reduced cysteine residues was confirmed, along with minor changes in proportions of keratin substructures.