Green function Retrieval and Time-reversal in a Disordered World

We apply the theory of multiple wave scattering to two contemporary, related topics: imaging with diffuse correlations and stability of time-reversal of diffuse waves, using equipartition, coherent backscattering and frequency speckles as fundamental concepts.Comment: 1 figur

Singular Perturbations In Option Pricing

After the celebrated Black-Scholes formula for pricing call options under constant volatility, the need for more general nonconstant volatility models in financial mathematics has been the motivation of numerous works during the Eighties and Nineties. In particular, a lot of attention has been paid to stochastic volatility models where the volatility is randomly fluctuating driven by an additional Brownian motion. We have shown in [2, 3] that, in the presence of a separation of time scales, between the main observed process and the volatility driving process, asymptotic methods are very efficient in capturing the effects of random volatility in simple robust corrections to constant volatility formulas. From the point of view of partial differential equations this method corresponds to a singular perturbation analysis. The aim of this paper is to deal with the nonsmoothness of the payoff function inherent to option pricing. We present the case of call options for which the payoff function forms an angle at the strike price. This case is important since these are the typical instruments used in the calibration of pricing models. We establish the pointwise accuracy of the corrected Black-Scholes price by using an appropriate payoff regularization which is removed simultaneously as the asymptotics is performed

Screen-printed multienzyme arrays for use in amperometric batch and flow systems

Screen-printing technology for electrode fabrication enables construction of amperometric devices suitable for combination of several enzyme electrodes. To develop a biosensor array for characterisation of wastewaters, tyrosinase and horseradish peroxidase (HRP) or cholinesterase-modified electrodes were combined on the same array. The behaviour of the tyrosinase-modified electrode in the presence of hydrogen peroxide (required co-substrate for the HRP-modified electrode) and acetylthiocholine chloride (required co-substrate for cholinesterase) was studied. Performance of bi-enzyme biosensor arrays in the batch mode and in the flow-injection system are discussed

Multienzyme electrochemical array sensor for determination of phenols and pesticides

The screen-printed four-electrode system was used as the amperometric transducer for determination of phenols and pesticides using immobilised tyrosinase. peroxidase. acetylcholinesterase and butyrylcholinesterase. Acetylthiocholine chloride was chosen as substrate for cholinesterases to measure inhibition by pesticides, hydrogen peroxide served as co-substrate for peroxidase to measure phenols. The compatibility of hydrolases and oxidoreductases working in the same array was studied. The detection of p-cresol, catechol and phenol as well as of pesticides including carbaryl, heptenophos and fenitrothion was carried out in flow-through and steady state arrangements. In addition. the effects of heavy metals (CL2+, Cd2+, Fe3+), fluoride (NaF), benzene and dimethylsulphoxide on cholinesterase activities ere evaluated. It was demonstrated that electrodes modified with hydrolases and oxidoreductases can function in the same array. The achieved R.S.D. values obtained for the flow system were below 4% for the same sensor and less than 10% within a group of five sensors. For the steady state system, R.S.D.s were approximately twice higher. One assay was completed in less than 6 min. The limit of detection for catechol Using tyrosinase was equal to 0.35 and 1.7 muM in the flow and steady state systems, respectively. On the contrary, lower limits of detection for pesticides were achieved in the steady state system-carbaryl 26 W, heptenophos 14 nM and fenitrothion 0.58 muM. (C) 2004 Elsevier B.V. All rights reserved

Amperometric screen-printed biosensor arrays with co-immobilised oxidoreductases and cholinesterases

Amperometric screen-printed biosensor arrays for detection of pesticides (organophosphates and carbamates) and phenols have been developed. Cholinesterases (AChE and BChE), tyrosinase (TYR), peroxidases (SBP. soybean and HRP. horseradish) and cellobiose dehydrogenase (CDH) were combined on the same array consisting of one Ag/AgCl reference electrode surrounded by eight radially distributed working electrodes of either carbon or platinum. Mainly cross-linking with glutaraldehyde was employed for enzyme immobilisation. The substrates for the enzymes were acetylthiocholine for cholinesterases (ChEs), cellobiose for CDH and hydrogen peroxide for peroxidases. Hydrogen peroxide was generated in the presence of glucose by co-immobilised glucose oxidase (GOx). All measurements were performed in an electrochemical steady state system specially constructed for eight channel screen-printed electrode arrays. The achieved relative standard deviation values calculated for different enzyme substrates (10 measurements) were typically below 7% and one assay was completed within less than 10 min. The detection limits for pesticides and phenols were in the nanomolar and micromolar ranges, respectively. The developed biosensor array was evaluated on wastewater samples. To simplify interpretation of results. the measured data were created with multivariate analysis-principal component analysis (PCA). (C) 2004 Elsevier B.V. All rights reserved