NAP enzyme recruitment in simultaneous bioremediation and nanoparticles synthesis.

Biotechnol Rep (Amst)

Environmental Biotechnology Department, Genetic Engineering and Biotechnology Research Institute, City of Scientific Research and Technological Applications, 21934 Borgelarab, Alexandria, Egypt.

Published: June 2018

AI Article Synopsis

  • The periplasmic nitrate reductase enzyme (NAP) has been identified as a promising catalyst for eco-friendly applications, particularly in bioremediation and nanoparticle synthesis.
  • The study explored the immobilization of denitrifying bacteria and NAP enzyme to enhance their effectiveness in harsh environments, achieving a notable reduction rate of NO and production of silver nanoparticles (AgNPs).
  • The results indicated that while immobilized bacteria effectively eliminated 100% of NO in 192 hours, the immobilized NAP enzyme showed lower efficiency, with only 28.6% NO reduction over 288 hours and larger aggregated AgNPs.

Article Abstract

The periplasmic nitrate reductase enzyme (NAP) has become attractive catalyst, whose exploitation has emerged as one of the indispensable strategies toward environmentally benign applications. To achieve them efficiently and overcome the sensitivity of NAP in harsh environmental circumstances, the immobilization for denitrifying bacteria and NAP enzyme for simultaneous bioremediation and bionanoparticles synthesis was studied. NAP catalyzed NO reduction at V of 0.811 μM/min and K of 14.02 mM. Concurrently, the immobilized MMT cells completely removed NO- upon 192 h with AgNPs synthesis ranging from 23.26 to 58.14 nm as indicated by SEM. Wherase, immobilized NAP exhibited lower efficiency with 28.6% of NO elimination within 288 h and large aggregated AgNPs ranging from 94.44 nm to 172.22 nm. To the best of author knowledge, the immobilization for denitrifying bacteria and NAP enzyme for simultaneous bioremediation and bionanoparticles synthesis was not studied before.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5989592PMC
http://dx.doi.org/10.1016/j.btre.2018.e00257DOI Listing

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