Acromed Invest AB

Lund, Sweden

Acromed Invest AB

Lund, Sweden
SEARCH FILTERS
Time filter
Source Type

Grant
Agency: European Commission | Branch: FP7 | Program: CP | Phase: OCEAN 2013.1 | Award Amount: 5.56M | Year: 2013

SMS will deliver a novel automated networked system that will enable real-time in situ monitoring of marine water chemical and ecological status in coastal areas by the detection of a series of contaminants regulated by the MSFD. SMS will design a multi-modular apparatus that will host in a single unitthe Main Box (MB)a Sampling Module and an Analysis Module. The former will contain sample collection and treatment components, whereas the latter will include four biosensor sub-modules that will enable detection and measurement of algal toxins and their associated algal species; several hazardous compounds (tributyltin, diuron and pentaBDPE); sulphonamides and a series of standard water quality parameters. The MB will be equipped with a communication module for real-time data transfer to a control center, where data processing will take place, enabling alarm functionality to Health Warning Systems, whenever some critical value exceeds a pre-defined threshold. It will be placed on a floating platform or buoy positioned in loco at defined locations. SMS will also develop a Specific Marine Pollution Metric that will combine real-time data of pollutant concentrations and water quality parameters, to produce a quantitative assessment of marine water quality. All work will culminate in showcasing the projects results in three demonstration sites: in La Spezia, Italy, in the Slovenian Adriatic Sea and in the Alonissos marine park in Greece. The consortium brings together skills from industry and academia to address the proposed work program. The record track of the partners is a strong indication that the project will achieve its ambitious objectives and make a lasting impact through its exploitation plan. The technology development and test cases bring together a multi-sectorial team of experts interacting with endusers and marine water stakeholders, demonstrating that ICT, biotechnology and nanotechnology can increase the potential of biosensors for marine applications


Ali S.M.U.,Linköping University | Ibupoto Z.H.,Linköping University | Salman S.,Acromed Invest AB | Nur O.,Linköping University | And 2 more authors.
Sensors and Actuators, B: Chemical | Year: 2011

Well-aligned zinc oxide (ZnO) nanowire arrays were fabricated on gold-coated plastic substrates using a low-temperature aqueous chemical growth (ACG) method. The ZnO nanowire arrays with 50-130 nm diameters and ∼1 μm in lengths were used in an enzyme-based urea sensor through immobilization of the enzyme urease that was found to be sensitive to urea concentrations from 0.1 mM to 100 mM. Two linear sensitivity regions were observed when the electrochemical responses (EMF) of the sensors were plotted vs. The logarithmic concentration range of urea from 0.1 mM to 100 mM. The proposed sensor showed a sensitivity of 52.8 mV/decade for 0.1-40 mM urea and a fast response time less than 4 s was achieved with good selectivity, reproducibility and negligible response to common interferents such as ascorbic acid and uric acid, glucose, K+ and Na+ ions. © 2011 Elsevier B.V. All rights reserved.


Israr M.Q.,Linköping University | Sadaf J.R.,Linköping University | Asif M.H.,Linköping University | Nur O.,Linköping University | And 3 more authors.
Thin Solid Films | Year: 2010

An electrochemical biosensor based on ZnO nanorods for potentiometric cholesterol determination is proposed. Hexagon-shaped ZnO nanorods were directly grown on a silver wire having a diameter of 250 μm using low temperature aqueous chemical approach that produced ZnO nanorods with a diameter of 125-250 nm and a length of ∼ 1 μm. Cholesterol oxidase (ChOx) was immobilized by a physical adsorption method onto ZnO nanorods. The electrochemical response of the ChOx/ZnO/Ag biosensor against a standard reference electrode (Ag/AgCl) was investigated as a logarithmic function of the cholesterol concentration (1 × 10-6 M to 1 × 10-2 M) showing good linearity with a sensitivity of 35.2 mV per decade and the stable output signal was attained at around 10 s. © 2010 Elsevier B.V. All rights reserved.


Israr M.Q.,Linköping University | Sadaf J.R.,Linköping University | Nur O.,Linköping University | Willander M.,Linköping University | And 3 more authors.
Applied Physics Letters | Year: 2011

Chemically fashioned zinc oxide (ZnO) nanowalls on aluminum wire have been characterized and utilized to fabricate a potentiometric cholesterol biosensor by an electrostatic conjugation with cholesterol oxidase. The sensitivity, specificity, reusability, and stability of the conjugated surface of ZnO nanowalls with thickness of ∼80 nm have been investigated over a wide logarithmic concentrations of cholesterol electrolyte solution ranging from 1× 10-6 -1× 10-3 M. The presented biosensor illustrates good linear sensitivity slope curve (∼53 mV/decade) corresponding to cholesterol concentrations along with rapid output response time of ∼5 s. © 2011 American Institute of Physics.


Pal S.,Biosensor Laboratory | Sharma M.K.,Indian Institute of Technology Delhi | Danielsson B.,Acromed Invest AB | Willander M.,Linköping University | And 2 more authors.
Biosensors and Bioelectronics | Year: 2014

A novel reusable chemiluminescence choline nanobiosensor has been developed using aligned zinc oxide nanorod-films (ZnONR). The chemically fashioned ZnONR were synthesized by hybrid wet chemical route onto glass substrates and used to fabricate a stable chemiluminescent choline biosensor. The biosensor was constructed by co-immobilization of the enzymes choline oxidase and peroxidase. The covalent immobilization of the enzymes on the ZnONR was achieved using 16-phosphonohexadecanoic acid as a cross-linker. The phosphonation of the ZnONR imparted significant stability to the immobilized enzyme as against physisorbed enzyme. A lower value of Michaelis-Menten constant (Km), of 0.062mM for the covalently coupled enzyme over the physisorbed enzymes facilitated enhanced stability of ZnONR nanobiosensor. The ZnONR-choline biosensor has been investigated over a wide range of choline from 0.0005mM to 2mM. Importantly, the recovery of choline in milk samples was close to 99%. Using the developed biosensor, choline was measurable even after 30 days with 60 repeated measurements proving the stability of the sensor (Intraday RSD%=2.83 and Interday RSD%=3.51). © 2013 Elsevier B.V.


Yakovleva M.,Lund University | Buzas O.,Lund University | Matsumura H.,Lund University | Matsumura H.,University of Tokyo | And 7 more authors.
Biosensors and Bioelectronics | Year: 2012

A novel method for lactose determination in milk is proposed. It is based on oxidation of lactose by cellobiose dehydrogenase (CDH) from the basidiomycete Phanerochaete chrysosporium, immobilised in an enzyme reactor. The reactor was prepared by cross-linking CDH onto aminopropyl-silanised controlled pore glass (CPG) beads using glutaraldehyde. The combined biosensor worked in flow injection analysis (FIA) mode and was developed for simultaneous monitoring of the thermometric signal associated with the enzymatic oxidation of lactose using p-benzoquinone as electron acceptor and the electrochemically generated current associated with the oxidation of the hydroquinone formed. A highly reproducible linear response for lactose was obtained between 0.05. mM and 30. mM. For a set of more than 500 samples an R.S.D. of less than 10% was achieved. The assay time was ca. 2. min per sample. The sensor was applied for the determination of lactose in dairy milk samples (milk with a fat content of 1.5% or 3% and also " lactose free" milk). No sample preparation except dilution with buffer was needed. The proposed method is rapid, suitable for repeated use and allows the possibility to compare results from two different detection methods, thus providing a built-in quality assurance. Some differences in the response observed between the methods indicate that the dual approach can be useful in mechanistic studies of redox enzymes. In addition, a dual system opens up interesting possibilities for studies of enzyme properties and mechanisms. © 2011 Elsevier B.V.


Fulati A.,Linköping University | Ali S.M.U.,Linköping University | Ali S.M.U.,NED University of Engineering and Technology | Asif M.H.,Linköping University | And 7 more authors.
Sensors and Actuators, B: Chemical | Year: 2010

In this study, a potentiometric intracellular glucose biosensor was fabricated by immobilization of glucose oxidase on nanoflake ZnO. Nanoflake ZnO with a wall thickness around 200 nm was grown on the tip of a borosilicate glass capillary and used as a selective intracellular glucose biosensor for the measurement of glucose concentrations in human adipocytes and frog oocytes. The results showed a fast response within 4 s and a logarithmic linear glucose-dependent electrochemical potential difference over a wide range of glucose concentration (500 nM-10 mM). Our measurements of intracellular glucose were consistent with the values of intracellular glucose concentrations reported in the literature. The monitoring capability of the sensor was demonstrated by following the increase in the intracellular glucose concentration induced by insulin in adipocytes and frog oocytes. In addition, the nanoflake ZnO material provided 1.8 times higher sensitivity than previously used ZnO nanorods under the same conditions. Moreover, the fabrication method in our experiment is simple and the resulting nanosensor showed good performance in sensitivity, stability, selectivity, reproducibility, and anti-interference. All these results demonstrate that the nanoflake ZnO can provide a promising material for reliable measurements of intracellular glucose concentrations within single living cells. © 2010 Elsevier B.V.


Safina G.,Lund University | Safina G.,Gothenburg University | Duran I.B.,Lund University | Alasel M.,Lund University | Danielsson B.,Acromed Invest AB
Talanta | Year: 2011

A study of specific interactions between lectins and glycoproteins has been carried out using surface plasmon resonance (SPR) in a flow-injection mode. Lectins were covalently immobilised on the surfaces of the microfluidic sensor chip via amine coupling and serum glycoproteins were injected into the flow channels. Specific lectin-glycoprotein interactions caused the shift of refractive index proportional to the mass concentration accumulated on the channel surface. Lectins showed different affinity to the tested glycoproteins and each glycoprotein displayed its own lectin-binding pattern. It is possible to distinguish and identify even glycoproteins with similar sugar structures by simple and quick screening. The working conditions of the assay were optimised. The lectin-based SPR made it possible to carry out the label-free detection of glycoproteins within a broad concentration range with a good linearity. Regeneration conditions for the surface of the sensor chip were found and optimised. Combination of 10 mM HCl and 10 mM glycine-HCl (pH 2.5) removes the bound glycoproteins from the lectin surface without damaging it. The kinetic and affinity parameters of lectin-glycoprotein binding were evaluated. The proposed method was tested on human glycosylated serum. Combination of the lectin panel with SPR is suitable both for specific screening and for sensitive assay of serum glycoproteins. © 2011 Elsevier B.V. All rights reserved.


Yakovleva M.E.,Lund University | Moran A.P.,National University of Ireland | Safina G.R.,Gothenburg University | Wadstrom T.,Lund University | Danielsson B.,Acromed Invest AB
Analytica Chimica Acta | Year: 2011

Seven Campylobacter jejuni strains were characterised by a lectin typing assay. The typing system was based on a quartz crystal microbalance technique (QCM) with four commercially available lectins (wheat germ agglutinin, Maackia amurensis lectin, Lens culinaris agglutinin, and Concanavalin A), which were chosen for their differing carbohydrate specificities. Initially, the gold surfaces of the quartz crystals were modified with 11-mercaptoundecanoic acid followed by lectin immobilisation using a conventional amine-coupling technique. Bacterial cells were applied for lectin typing without preliminary treatment, and resonant frequency and dissipation responses were recorded. The adhesion of microorganisms on lectin surfaces was confirmed by atomic force microscopy. Scanning was performed in the tapping mode and the presence of bacteria on lectin-coated surfaces was successfully demonstrated. A significant difference in the dissipation response was observed for different C. jejuni strains which made it possible to use this parameter for discriminating between bacterial strains. In summary, the QCM technique proved a powerful tool for the recognition and discrimination of C. jejuni strains. The approach may also prove applicable to strain discrimination of other bacterial species, particularly pathogens. © 2011 Elsevier B.V.


Yakovleva M.,Lund University | Bhand S.,Birla Institute of Technology and Science | Danielsson B.,Acromed Invest AB
Analytica Chimica Acta | Year: 2013

This review describes principles and features of thermal biosensors and microbiosensors in flow injection analysis. Examples are given that illustrate the great versatility and excellent operational stability offered by thermal biosensors. The examples are mostly from work with the original type of enzyme thermistor operating with an enzyme column, but there will also be work described involving miniaturised devices including thermal lab-on-chip constructions and other types of sensing materials, such as MIPs (molecularly imprinted polymers) for both affinity and catalytic reactions. Several recently presented thermal biosensor concepts are reviewed including a thermal-electrochemical hybrid sensor for lactose based on immobilised cellobiose dehydrogenase. Another recent method is the determination of fructose using a fructose-6-phosphate kinase column. Operation with complex sample matrices such as blood, plasma and milk and how to avoid non-specific temperature effects are considered. © 2012 Elsevier B.V.

Loading Acromed Invest AB collaborators
Loading Acromed Invest AB collaborators