Khardenavis, Anshuman and Kapley, Atya and Purohit, H J (2009) Processing of poultry feathers by alkaline keratin hydrolyzing enzyme from Serratia sp. HPC 1383. Waste Management, 29. pp. 1409-1415. ISSN 0956-053X

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The present study describes the production and characterization of a feather hydrolyzing enzyme by Serratia sp. HPC 1383 isolated from tannery sludge, which was identified by the ability to form clear zones around colonies on milk agar plates. The proteolytic activity was expressed in terms of the micromoles of tyrosine released from substrate casein per ml per min (U/mL min). Induction of the inoculum with protein was essential to stimulate higher activity of the enzyme, with 0.03% feathermeal in the inoculum resulting in increased enzyme activity (45 U/mL) that further increased to 90 U/mL when 3 d old inoculum was used. The highest enzyme activity, 130 U/mL, was observed in the presence of 0.2% yeast extract. The optimum assay temperature and pH for the enzyme were found to be 60 �C and 10.0, respectively. The enzyme had a half-life of 10 min at 60 �C, which improved slightly to 18 min in presence of 1 mM Ca2+. Inhibition of the enzyme by phenylmethyl sulfonyl fluoride (PMSF) indicated that the enzyme was a serine protease. The enzyme was also partially inhibited (39%) by the reducing agent b-mercaptoethanol and by divalent metal ions such as Zn2+ (41% inhibition). However, Ca2+ and Fe2+ resulted in increases in enzyme activity of 15% and 26%, respectively. The kinetic constants of the keratinase were found to be 3.84 lM (Km) and 108.7 lM/mL min (Vmax). These results suggest that this extracellular keratinase may be a useful alternative and eco-friendly route for handling the abundant amount of waste feathers or for applications in other industrial processes.

Item Type: Article
Subjects: Solid Waste Treatment & Disposal
Waste Utilization
Environmental Resources, Conservation
Environmental Biotechnology
Depositing User: Dr Anshuman Khardenavis
Date Deposited: 31 Mar 2017 10:06
Last Modified: 09 May 2017 09:09

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