Keratinases from Streptomyces netropsis and Bacillus subtilis and Their Potential Use in the Chicken Feather Degrading

Author:

Abdelmoteleb Ali1,Gonzalez-Mendoza Daniel2,Tzintzun-Camacho Olivia2ORCID,Grimaldo-Juárez Onecimo2ORCID,Mendez-Trujillo Vianey3,Moreno-Cruz Carlos2,Ceceña-Duran Carlos2,Roumia Ahmed4ORCID

Affiliation:

1. Botany Department, Faculty of Agriculture, Menoufia University, Shibin El-Kom 32514, Egypt

2. Institute of Agricultural Sciences, Autonomous University of Baja California (ICA-UABC), Highway to Delta s/n C.P, Ejido Nuevo León 21705, Baja California, Mexico

3. Faculty of Medicine, Autonomous University of Baja California, Dr. Humberto Torres Sanginés S/N, Centro Cívico, Mexicali 21000, Baja California, Mexico

4. Department of Agricultural Biochemistry, Faculty of Agriculture, Menoufia University, Shibin El-Kom 32514, Egypt

Abstract

Feathers are the most prevalent agricultural waste generated by chicken farms, polluting the environment and wasting protein resources as a result of the accumulation of large amounts of feathers. Therefore, keratinase-producing microorganisms represent a promising potential technique for the degradation of feather waste. Streptomyces netropsis A-ICA and Bacillus subtilis ALICA, previously isolated from the rhizosphere of desert plants (Larrea tridentata and Prosopis juliflora) respectively, were assessed for their feather-degradation ability. Keratinase activity was optimized using various parameters, including incubation time, pH, temperature, and feather concentration. The maximum keratinase activity of S. netropsis A-ICA and B. subtilis ALICA (113.6 ± 5.1 and 135.6 ± 4.1 U/mL) was obtained at the 5th and 3rd day of incubation with initial pH of 7.0 and 7.5 at 25 and 30 °C, and 1% (w/v) of chicken feather, respectively. Under the optimized conditions, the concentration of soluble protein in the feather hydrolysate reached 423.3 ± 25 and 565.3 ± 7.7 µg/mL, with feathers weight loss of 84 ± 2 and 86± 1.5% by S. netropsis A-ICA and B. subtilis ALICA, respectively. The highest disulphide bond reductase activity reached 10.7 ± 0.4 and 10.96 ± 1.1 U/mL, after five and three days of inoculation with S. netropsis A-ICA and B. subtilis ALICA, respectively. Furthermore, the antioxidant activity of feather protein hydrolysate obtained by S. netropsis A-ICA and B. subtilis ALICA was evaluated using DPPH radical-scavenging activity, which exhibited a significant antioxidant potential with an IC50 value of 0.8 and 0.6 mg/mL. The 3D models of detected keratinases in both strains showed high similarity with subtilisin family. Further, the docking results clarified the importance of GSG and VVVFTP domains in B. subtilis and beta-keratin, respectively. The present study revealed the keratinolytic potential of S. netropsis A-ICA and B. subtilis ALICA in chicken feather degradation, which have potential application value and may be exploited as supplementary protein and antioxidant in animal feed formulations.

Publisher

MDPI AG

Subject

Plant Science,Biochemistry, Genetics and Molecular Biology (miscellaneous),Food Science

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