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Investigators at University of Connecticut Report Findings in Enzymes and Coenzymes (Biofunctionalization of alpha-Zirconium Phosphate Nanosheets:...

August 5, 2014



Investigators at University of Connecticut Report Findings in Enzymes and Coenzymes (Biofunctionalization of alpha-Zirconium Phosphate Nanosheets: Toward Rational Control of Enzyme Loading, Affinities, Activities and Structure Retention)

By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Enzymes and Coenzymes. According to news reporting out of Storrs, Connecticut, by NewsRx editors, research stated, "Controlling the properties of enzymes bound to solid surfaces in a rational manner is a grand challenge. Here we show that preadsorption of cationized bovine serum albumin (cBSA) to alpha-Zr(IV) phosphate (alpha-ZrP) nanosheets promotes enzyme binding in a predictable manner, and surprisingly, the enzyme binding is linearly proportional to the number of residues present in the enzyme or its volume, providing a powerful, new predictable tool."

Our news journalists obtained a quote from the research from the University of Connecticut, "The cBSA loaded alpha-ZrP (denoted as bZrP) was tested for the binding of pepsin, glucose oxidase (GOX), tyrosinase, catalase, myoglobin and laccase where the number of residues increased from the lowest value of similar to 153 to the highest value of 2024. Loading depended linearly on the number of residues, rather than enzyme charge or its isoelectric point. No such correlation was seen for the binding of these enzymes to alpha-ZrP nanosheets without the preadsorption of cBSA, under similar conditions of pH and buffer. Enzyme binding to bZrP was supported by centrifugation studies, powder X-ray diffraction and scanning electron microscopy/energy-dispersive X-ray spectroscopy. All the bound enzymes retained their secondary structure and the extent of structure retention depended directly on the amount of cBSA preadsorbed on alpha-ZrP, prior to enzyme loading. Except for tyrosinase, all enzyme/bZrP biocatalysts retained their enzymatic activities nearly 90-100%, and biofunctionalization enhanced the loading, improved structure retention and supported higher enzymatic activities."

According to the news editors, the research concluded: "This approach of using a chemically modified protein to serve as a glue, with a predictable affinity/loading of the enzymes, could be useful to rationally control enzyme binding for applications in advanced biocatalysis and biomedical applications."

For more information on this research see: Biofunctionalization of alpha-Zirconium Phosphate Nanosheets: Toward Rational Control of Enzyme Loading, Affinities, Activities and Structure Retention. ACS Applied Materials & Interfaces, 2014;6(12):9643-9653. ACS Applied Materials & Interfaces can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; ACS Applied Materials & Interfaces - www.pubs.acs.org/journal/aamick)

Our news journalists report that additional information may be obtained by contacting I.K. Deshapriya, University of Connecticut, Dept. of Mol & Cell Biol, Storrs, CT 06269, United States. Additional authors for this research include C.S. Kim, M.J. Novak and C.V. Kumar (see also Enzymes and Coenzymes).

Keywords for this news article include: Storrs, Anions, Nanosheets, Phosphates, Tyrosinase, Connecticut, United States, Nanotechnology, Phosphoric Acids, Emerging Technologies, Enzymes and Coenzymes, North and Central America

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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