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Hyderabad, India

Kanugula A.K.R.,University of Hyderabad | Repalle E.R.,University of Hyderabad | Pandey J.P.,University of Hyderabad | Sripad G.,Virchow Biotech Pvt. Ltd | And 3 more authors.
Indian Journal of Geo-Marine Sciences | Year: 2011

Bacterial organophosphate hydrolases (OPH) have been shown to hydrolyze structurally diverse group of organophosphate (OP) compounds and nerve agents. Due to broad substrate range and unusual catalytic properties, the OPH has successfully been used to develop eco-friendly strategies for detection and decontamination of OP compounds. However, their usage has failed to gain necessary acceptance, due to short half-life of the enzyme and loss of activity during process development. In the present study, we report a simple procedure for immobilization of OPH on biocompatible gelatin pads. The covalent coupling of OPH using glutaraldehyde spacer has been found to dramatically improve the enzyme stability. There is no apparent loss of OPH activity in OPH-gelatin pads stored at room temperature for more than six months. As revealed by a number of kinetic parameters, the catalytic properties of immobilized enzyme are found to be comparable to the free enzyme. Further, the OPH-gelatin pads effectively eliminate OP insecticide methyl parathion and nerve agent sarin. © 2011, National Institute of Science Communication and Information Resources (NISCAIR). All rights reserved.

Kalugonda M.K.,Virchow Biotech Pvt. Ltd | Venkateswarulu T.C.,Vignan University | Kosana R.R.,Virchow Biotech Pvt. Ltd | Bajjji C.,Virchow Biotech Pvt. Ltd | And 5 more authors.
International Journal of Pharma and Bio Sciences | Year: 2013

Tumor Lysis Syndrome and Gout are the conditions in which uric acid levels in the serum will be increased up to 526 mg/dl but in a healthy human being the uric acid concentration is less than 15mg/dl. In such conditions urate oxidase can be administered parentrally which can solublise the uric acid in to allontoin which has 3 to 5 fold more solubility than uric acid and it can be excreted through urine and maintain the uric acid concentration at normal level. In this article urate oxidase gene was isolated Aspergillus flavus and it was cloned in to E. coli (BL-21). Urate oxidase gene was expressed in the cytoplasm as soluble and biologically active form. Bioprocess was optimized for 20lts fermenter scale with modified LB medium and purified up to >96% purity using fractionated ammonium sulphate precipitation, diafiltration, anion exchange chromatography, cation exchange chromatography and gel filtration chromatography. The final yield of purified recombinant urate oxidase from the 20lts fermenter was approximately 5 to 6gm of 96% pure and biologically active enzyme.

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