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Greta Faccio  - - - 
Top co-authors
Linda Thöny-Meyer

41 shared publications

Laboratory for Biointerfaces, Empa, Swiss Federal Laboratories for Materials Science and Technology, Lerchenfeldstrasse 5, CH-9014 St. Gallen, Switzerland

Michael Richter

14 shared publications

Fraunhofer Institute for Interfacial Engineering and Biotechnology IGB; Bio, Electro and Chemocatalysis BioCat; Straubing branch; Schulgasse 11a 94315 Straubing Germany

Renate Reiss

6 shared publications

Empa. Swiss Federal Laboratories for Materials Science and Technology, Laboratory for Biomaterials, Lerchenfeldstr. 5, 9014 St. Gallen, Switzerland

36
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220
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Publication Record
Distribution of Articles published per year 
(2009 - 2018)
Total number of journals
published in
 
26
 
Publications See all
Article 0 Reads 3 Citations Plasma polymer film designs through the eyes of ToF-SIMS Laetitia Bernard, Patrick Rupper, Greta Faccio, Dirk Hegeman... Published: 01 June 2018
Biointerphases, doi: 10.1116/1.5016046
DOI See at publisher website
Article 0 Reads 2 Citations Enhanced Antimicrobial Activity and Structural Transitions of a Nanofibrillated Cellulose–Nisin Biocomposite Suspension Ramon Weishaupt, Lukas Heuberger, Gilberto Siqueira, Beatric... Published: 16 May 2018
ACS Applied Materials & Interfaces, doi: 10.1021/acsami.8b04470
DOI See at publisher website
Article 0 Reads 0 Citations Near-Surface Structure of Plasma Polymer Films Affects Surface Behavior in Water and its Interaction with Proteins Marianne Vandenbossche, Gesine Gunkel-Grabole, Anja Car, Lae... Published: 02 May 2018
Plasma Chemistry and Plasma Processing, doi: 10.1007/s11090-018-9897-z
DOI See at publisher website
Article 1 Read 0 Citations From Protein Features to Sensing Surfaces. Greta Faccio Published: 15 April 2018
Sensors,
PubMed View at PubMed ABS Show/hide abstract
Proteins play a major role in biosensors in which they provide catalytic activity and specificity in molecular recognition. However, the immobilization process is far from straightforward as it often affects the protein functionality. Extensive interaction of the protein with the surface or significant surface crowding can lead to changes in the mobility and conformation of the protein structure. This review will provide insights as to how an analysis of the physico-chemical features of the protein surface before the immobilization process can help to identify the optimal immobilization approach. Such an analysis can help to preserve the functionality of the protein when on a biosensor surface.
Article 1 Read 1 Citation From Protein Features to Sensing Surfaces Greta Faccio Published: 15 April 2018
Sensors, doi: 10.3390/s18041204
DOI See at publisher website ABS Show/hide abstract
Proteins play a major role in biosensors in which they provide catalytic activity and specificity in molecular recognition. However, the immobilization process is far from straightforward as it often affects the protein functionality. Extensive interaction of the protein with the surface or significant surface crowding can lead to changes in the mobility and conformation of the protein structure. This review will provide insights as to how an analysis of the physico-chemical features of the protein surface before the immobilization process can help to identify the optimal immobilization approach. Such an analysis can help to preserve the functionality of the protein when on a biosensor surface.
Article 0 Reads 0 Citations Characterization of sulfhydryl oxidase from Aspergillus tubingensis. Outi Nivala, Greta Faccio, Mikko Arvas, Perttu Permi, Johann... Published: 08 December 2017
BMC Biochemistry, doi: 10.1186/s12858-017-0090-4
DOI See at publisher website PubMed View at PubMed ABS Show/hide abstract
Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initial activity was retained after incubation at 50 °C for 20 h. AtSOX contains a non-covalently bound flavin cofactor. The enzyme oxidised a sulfhydryl group of glutathione to form a disulfide bond, as verified by nuclear magnetic resonance spectroscopy. AtSOX preferred glutathione as a substrate over cysteine and dithiothreitol. The activity of the enzyme was totally inhibited by 10 mM zinc sulphate. Peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, were not oxidised by the enzyme. Based on the analysis of 33 fungal genomes, SOX enzyme encoding genes were found close to nonribosomal peptide synthetases (NRPS) but not with polyketide synthases (PKS). In the phylogenetic tree, constructed from 25 SOX and thioredoxin reductase sequences from IPR000103 InterPro family, AtSOX was evolutionary closely related to other Aspergillus SOXs. Oxidoreductases involved in the maturation of nonribosomal peptides of fungal and bacterial origin, namely GliT, HlmI and DepH, were also evolutionary closely related to AtSOX whereas fungal thioreductases were more distant. AtSOX (55 kDa) is a fungal secreted flavin-dependent enzyme with good stability to both pH and temperature. A Michaelis-Menten behaviour was observed with reduced glutathione as a substrate. Based on the location of SOX enzyme encoding genes close to NRPSs, SOXs could be involved in the secondary metabolism and act as an accessory enzyme in the production of nonribosomal peptides.
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