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CL Lin

Publications and source records attributed to CL Lin.

At least 19 recordsLinked to original sources

Lattice boltzmann method on composite grids

A composite block-structured lattice Boltzmann method is proposed for the simulation of two-dimensional incompressible fluid flows. The grid structure is composed of a coarse base grid and one or several fine grid(s). The former covers the entire physical domain; the latter are placed at regions where local grid refinement is desirable. The simulation is first carried out on the base grid level at a smaller relaxation time, allowing a rapid propagation of boundary information throughout the entire domain. Thus large-scale flow features can be resolved efficiently at a relatively low cost. At a later time, fine grid variables are initiated. The dependent variables on both grid levels are, then, advanced in time simultaneously with the fine grid boundary conditions obtained from the base grid solution at the grid interface. As a demonstration, the lid-driven cavity flow is selected for study. The results show good agreement with benchmark numerical data and those calculated from the finite-volume U2RANS model. The proposed method is able to produce accurate solutions on fine grids, with a considerable saving in CPU time.

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Purification and Characterization of an Extracellular beta-Glucosidase II with High Hydrolysis and Transglucosylation Activities from Aspergillus niger.

An extracellular beta-glucosidase II (beta-Glu II) has been purified to homogeneity by column chromatography from Aspergillus niger CCRC 31494. Its molecular mass was estimated to be 360 kDa by gel filtration and 120 kDa by SDS-PAGE. The enzyme has a pI of 4.0 and has optimum activity at pH 4.5 and 60 degrees C. The beta-Glu II was completely inhibited by 5.0 mM Fe(2+). Methanol (20%, v/v) activated the enzyme activity at 1.8-fold. V(max) values of 10.2 and 464 units/mg were found for p-nitrophenyl beta-D-glucoside (K(m) = 2.2 mM) and for cellobiose (K(m) = 15.4 mM). The enzyme was strongly inhibited by substrates, p-nitrophenyl beta-D-glucopyranoside in excess of 7.5 mM and cellobiose in excess of 50 mM, and was competitively inhibited by glucose with a K(i) of 5.7 mM. Transglucosylation products of cellotriose, methyl beta-glucoside and ethyl beta-glucoside, were obtained under neutral conditions and in the presence of methanol and ethanol, respectively.

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