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Isolation of a novel feather-degrading Ectobacillus sp. JY-23 strain and characterization of a new keratinase in the M4 metalloprotease family.
Peng, Shuaiying; Li, Hanguang; Zhang, Shuaiwen; Zhang, Rong; Cheng, Xin; Li, Kuntai.
Afiliación
  • Peng S; Jiangxi Engineering Laboratory for the Development and Utilization of Agricultural Microbial Resources, Jiangxi Agricultural University, Nanchang 330045, China.
  • Li H; Jiangxi Engineering Laboratory for the Development and Utilization of Agricultural Microbial Resources, Jiangxi Agricultural University, Nanchang 330045, China.
  • Zhang S; Jiangxi Engineering Laboratory for the Development and Utilization of Agricultural Microbial Resources, Jiangxi Agricultural University, Nanchang 330045, China.
  • Zhang R; Jiangxi Engineering Laboratory for the Development and Utilization of Agricultural Microbial Resources, Jiangxi Agricultural University, Nanchang 330045, China.
  • Cheng X; Jiangxi Engineering Laboratory for the Development and Utilization of Agricultural Microbial Resources, Jiangxi Agricultural University, Nanchang 330045, China.
  • Li K; College of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Key Labo
Microbiol Res ; 274: 127439, 2023 Sep.
Article en En | MEDLINE | ID: mdl-37364416
Microbial keratinases have prominent potential in biotransformation of recalcitrant keratin substrates to value-added products which has made keratinases a research focus in the past decades. In this study, an efficient feather-degrading bacterium was isolated and identified as a novel species in Ectobacillus genus and designated as Ectobacillus sp. JY-23. The degradation characteristics analysis revealed that Ectobacillus sp. JY-23 could utilize chicken feathers (0.4% w/v) as the sole nutrient source and degraded 92.95% of feathers in 72 h. A significant increase in sulfite and free sulfydryl group content detected in the feather hydrolysate (culture supernatant) indicated efficient reduction of disulfide bonds, which inferred that the degradation mechanism of isolated strain was a synergetic action of sulfitolysis and proteolysis. Moreover, abundant amino acids were also detected, among which proline and glycine were the predominant free amino acids. Then, the keratinase of Ectobacillus sp. JY-23 was mined and Y1_15990 was identified as the keratinase encoding gene of Ectobacillus sp. JY-23 and designated as kerJY-23. Escherichia coli strain overexpressing kerJY-23 degraded chicken feathers in 48 h. Finally, bioinformatics prediction of KerJY-23 demonstrated that it belonged to the M4 metalloprotease family, which was a third keratinase member in this family. KerJY-23 showed low sequence identity to the other two keratinase members, indicating the novelty of KerJY-23. Overall, this study presents a novel feather-degrading bacterium and a new keratinase in the M4 metalloprotease family with remarkable potential in feather keratin valorization.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pollos / Plumas Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Microbiol Res Asunto de la revista: MICROBIOLOGIA / SAUDE AMBIENTAL Año: 2023 Tipo del documento: Article País de afiliación: China Pais de publicación: Alemania

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pollos / Plumas Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Microbiol Res Asunto de la revista: MICROBIOLOGIA / SAUDE AMBIENTAL Año: 2023 Tipo del documento: Article País de afiliación: China Pais de publicación: Alemania