Biotransformation of keratin waste to amino acids and active peptides based on cell-free catalysis.

BACKGROUND: Keratin is the primary constituent of the vertebrate epidermis and epidermal appendages, as well as the main waste product generated during poultry processing from feathers, hair, scales, nails, etc. Keratin is generally hard, stubborn and difficult to hydrolyze; however, it is also inexpensive and contains more than 85% protein. Currently, tens of millions of tons of keratin waste are produced each year worldwide; however, no effective methods for the recovery of keratin waste have been reported thus far, making such research urgent. Keratinase has been reported to be useful for keratin waste recovery; however, nearly all keratinases are unable to hydrolyze keratin after they are detached from living cell systems. This may be due to low keratinase activity and lack of synergistic factors. RESULTS: Herein, the keratinase gene from Bacillus licheniformis BBE11-1 was successfully expressed in Bacillus subtilis WB600, allowing for improved activity of the recombinant keratinase KerZ1 to 45.14 KU/mL via promoter substitution and screening of the ribosome-binding sites. Further, real-time control of temperature, pH, dissolved oxygen, and feed strategy allowed the activity of KerZ1 to reach 426.60 KU/mL in a 15-L fermenter, accounting for a 3552-fold increase compared to the wild-type keratinase (120.1 U/mL). Most importantly, we proposed a method based on the synergistic action of keratinase KerZ1 and sodium sulfite, to hydrolyze feathers into amino acids. In specific, 100 g/L of feather waste can be successfully converted into 56.6% amino acids within 12 h, while supporting the production of dozens of bioactive peptides. CONCLUSIONS: The activity of recombinant keratinase can be greatly enhanced via transcription and translational regulation in Bacillus subtilis. The synergistic action of keratinase and sulfite can rapidly degrade feather waste and produce amino acids and polypeptides.

Effective biodegradation of chicken feather waste by co-cultivation of keratinase producing strains.

BACKGROUND: Chicken feather, a byproduct of poultry-processing industries, are considered a potential high-quality protein supplement owing to their crude protein content of more than 85%. Nonetheless, chicken feathers have been classified as waste because of the lack of effective recycling methods. In our previous studies, Bacillus licheniformis BBE11-1 and Stenotrophomonas maltophilia BBE11-1 have been shown to have feather-degrading capabilities in the qualitative phase. To efficiently recycle chicken feather waste, in this study, we investigated the characteristics of feather degradation by B. licheniformis BBE11-1 and S. maltophilia BBE11-1. In addition, in an analysis of the respective advantages of the two degradation systems, cocultivation was found to improve the efficiency of chicken feather waste degradation. RESULTS: B. licheniformis BBE11-1 and S. maltophilia BBE11-1 were used to degrade 50 g/L chicken feather waste in batches, and the degradation rates were 35.4% and 22.8% in 96 h, respectively. The degradation rate of the coculture system reached 55.2% because of higher keratinase and protease activities. Furthermore, cocultivation was conducted in a 3 L fermenter by integrating dissolved oxygen control and a two-stage temperature control strategy. Thus, the degradation rate was greatly increased to 81.8%, and the conversion rate was 70.0% in 48 h. The hydrolysates exhibited antioxidant activity and contained large quantities of amino acids (895.89 mg/L) and soluble peptides. CONCLUSIONS: Cocultivation of B. licheniformis BBE11-1 and S. maltophilia BBE11-1 can efficiently degrade 50 g/L chicken feather waste and produce large amounts of amino acids and antioxidant substances at a conversion rate of 70.0%.