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Wear particles in the lubrication oil of machinery contain a considerable amount of information about the level of wear in the machinery components, which can provide very early warnings of faults. Inductive debris sensors play an important role in online oil debris detecting techniques. A large unbalance voltage in the sensing coil induced by the asymmetry of two excitation coils harms the performance of a triple-coil inductive debris sensor. This work proposes an effective signal processing system which contributes to the establishment of a high-performance triple-coil inductive debris sensor. Several experiments are conducted to test the sensor’s detection performance. The results show that the sensor is sensitive, and can effectively detect 134 µm (D) ferrous particles and 230 µm (D) nonferrous particles in a sensing channel with an inner diameter of 43 mm.

This paper presents a novel approach to the investigation of the efficiency of Brownian motors in the framework of nonequilibrium theory. We derive an explicit expression of the entropy production rate (EPR) for a chemically driven Brownian motor and use this to develop an expression for motor efficiency in terms of the EPR. Our result is consistent with earlier derivations but is more general and physically transparent and thus applicable to a wider range of biological motors.Introduction. -Many active processes in biology, such as muscular contraction [1] and various cellular transport processes [2], are performed by a certain kind of enzyme called a molecular motor that moves in one direction along a periodic, polar filament by transducing chemical energy (usually from the catalysis of ATP into ADP · Pi) into mechanical work. These molecular motors are dominated by thermal motion and viscous forces and can be understood by modelling them as Brownian particles whose direction is derived from nonequilibrium fluctuations in an asymmetric potential [3][4][5][6][7].During ATP hydrolyzing reaction, the motor, denoted as M, will undergo the following states of nucleotide binding:

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