Literature DB >> 26920479

The 46 kDa dimeric protein from Variovorax paradoxus shows faster methotrexate degrading activity in its nanoform compare to the native enzyme.

Venkata Krishna Bayineni1, Krishna Venkatesh1, Chandan Kumar Sahu1, Ravi-Kumar Kadeppagari2.   

Abstract

Methotrexate degrading enzymes are required to overcome the toxicity of the methotrexate while treating the cancer. The enzyme from Variovorax paradoxus converts the methotrexate in to non toxic products. Methotrexate degrading enzyme from V. paradoxus is a dimeric protein with a molecular mass of 46 kDa and it acts on casein and gelatin. This enzyme is optimally active at pH 7.5 and 40°C and nanoparticles of this enzyme were prepared by desolvation-crosslinking method. Enzyme nanoparticles could degrade methotrexate faster than the native enzyme and they show lower Km compare to the native enzyme. Enzyme nanoparticles show better thermostability and they were stable for much longer time in the serum compare to the native enzyme. Enzyme nanoparticles show better functionality than the native enzyme while clearing the methotrexate added to the serum suggesting their advantage over the native enzyme for the therapeutic and biotechnological applications.
Copyright © 2016 Elsevier Inc. All rights reserved.

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Keywords:  Cancer; Casein; Enzyme nanoparticles; Gelatin; Methotrexate; Variovorax paradoxus

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Year:  2016        PMID: 26920479     DOI: 10.1016/j.enzmictec.2016.01.005

Source DB:  PubMed          Journal:  Enzyme Microb Technol        ISSN: 0141-0229            Impact factor:   3.493


  1 in total

1.  Characterization of a Stable Form of Carboxypeptidase G2 (Glucarpidase), a Potential Biobetter Variant, From Acinetobacter sp. 263903-1.

Authors:  Issa Sadeghian; Shiva Hemmati
Journal:  Mol Biotechnol       Date:  2021-07-15       Impact factor: 2.695

  1 in total

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