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Biodegradation of feather waste by keratinase produced from newly isolated Bacillus licheniformis ALW1.
Abdel-Fattah, Azza M; El-Gamal, Mamdouh S; Ismail, Siham A; Emran, Mohamed A; Hashem, Amal M.
Afiliación
  • Abdel-Fattah AM; Department of Chemistry of Natural and Microbial Products, Division of Pharmaceutical and Drug Industries Research, National Research Centre, Giza, Egypt.
  • El-Gamal MS; Department of Botany and Microbiology, Faculty of Science (Boys), Al-Azhar University, Cairo, Egypt.
  • Ismail SA; Department of Chemistry of Natural and Microbial Products, Division of Pharmaceutical and Drug Industries Research, National Research Centre, Giza, Egypt.
  • Emran MA; Department of Chemistry of Natural and Microbial Products, Division of Pharmaceutical and Drug Industries Research, National Research Centre, Giza, Egypt.
  • Hashem AM; Department of Chemistry of Natural and Microbial Products, Division of Pharmaceutical and Drug Industries Research, National Research Centre, Giza, Egypt.
J Genet Eng Biotechnol ; 16(2): 311-318, 2018 Dec.
Article en En | MEDLINE | ID: mdl-30733740
Keratinase are proteolytic enzymes which have gained much attention to convert keratinous wastes that cause huge environmental pollution problems. Ten microbial isolates were screened for their keratinase production. The most potent isolate produce 25.2 U/ml under static condition and was primarily identified by partial 16s rRNA gene sequence as Bacillus licheniformis ALW1. Optimization studies for the fermentation conditions increased the keratinase biosynthesis to 72.2 U/ml (2.9-fold). The crude extracellular keratinase was optimally active at pH 8.0 and temperature 65 °C with 0.7% soluble keratin as substrate. The produced B. licheniformis ALW1 keratinase exhibited a good stability over pH range from 7 to 9 and over a temperature range 50-60 °C for almost 90 min. The crude enzyme solution was able to degrade native feather up to 63% in redox free system.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Genet Eng Biotechnol Año: 2018 Tipo del documento: Article País de afiliación: Egipto Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Genet Eng Biotechnol Año: 2018 Tipo del documento: Article País de afiliación: Egipto Pais de publicación: Países Bajos