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Study Findings from University of Milan Provide New Insights into Enzymes and Coenzymes (Nanoscale Roughness Affects the Activity of Enzymes Adsorbed...

July 4, 2014



Study Findings from University of Milan Provide New Insights into Enzymes and Coenzymes (Nanoscale Roughness Affects the Activity of Enzymes Adsorbed on Cluster-Assembled Titania Films)

By a News Reporter-Staff News Editor at Science Letter -- Research findings on Enzymes and Coenzymes are discussed in a new report. According to news reporting originating from Milan, Italy, by NewsRx correspondents, research stated, "In this study, we investigated how the adsorption properties governed by the nanometer-scale surface morphology of cluster-assembled titanium oxide films influence the catalytic activity of immobilized serine-protease trypsin. We developed an activity assay for the parallel detection of physisorbed enzyme activity and mass density of the adsorbed proteins in microarray format."

Our news editors obtained a quote from the research from the University of Milan, "The method combines a microarray-based technique and advanced quantitative confocal microscopy approaches based on fluorescent labeling of enzymes and covalent labeling of active sites of surface-bound enzymes. The observed diminishing trypsin binding affinity with increasing roughness, as opposed to the steep rise in its saturation uptake, was interpreted as heterogeneous nucleation-driven adsorption of trypsin at the rough nanoporous titania surface. The increase in relative activity of adsorbed trypsin is proportional to the fractional saturation of titania surfaces, expressed as percentage of saturation uptake. In turn, the specific activity, that is, the ratio of active proteins to the absolute number of adsorbed proteins, drops with growing saturation uptake and surface roughness, witnessing a reduction in the accessibility of enzyme active sites. Both geometrical constraints of titania nanopores and the clusterwise adsorption of trypsin were identified as the key factors underpinning the steric hindrance of the immobilized enzyme. These findings are relevant for the optimization of rough nanoporous surfaces as carriers of immobilized enzymes."

According to the news editors, the research concluded: "The proposed activity assay is particularly advantageous in the screening of candidate materials for enzyme immobilization."

For more information on this research see: Nanoscale Roughness Affects the Activity of Enzymes Adsorbed on Cluster-Assembled Titania Films. Langmuir, 2014;30(20):5973-5981. Langmuir can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Langmuir - www.pubs.acs.org/journal/langd5)

The news editors report that additional information may be obtained by contacting L. Gailite, University of Milan, Dept. of Vet Sci & Public Hlth DIVET, I-20133 Milan, Italy. Additional authors for this research include P.E. Scopelliti, V.K. Sharma, M. Indrieri, A. Podesta, G. Tedeschi and P. Milani (see also Enzymes and Coenzymes).

Keywords for this news article include: Milan, Italy, Europe, Nanoscale, Nanoporous, Nanotechnology, Emerging Technologies, Enzymes and Coenzymes

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


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Source: Science Letter


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