Quantifying minimum monolith size and solute dilution from multi-compartment percolation sampler data

Preferential flow affects solute transport in natural soils, leading to high spatiotemporal variation of concentration. A multicompartment solute sampler (MCS), yielding multiple breakthrough curves at a given depth, can monitor tracer movement in a heterogeneous soil. We present a technique to estimate from MCS data whether a soil monolith is sufficiently large to capture preferential flow, which is a necessity for tracer breakthrough curves to be representative. For several soils, we estimate that an MCS should be larger than 0.1 to 0.2 m². We also expand dilution theory to analyze the concentration variations of a tracer passing the control plane monitored by the MCS, in addition to the conventional plume spreading analysis. We characterize the set of locally observed breakthrough curves by the entropy-based dilution index. For given first and second-central moment, the spatially uniform log-normal breakthrough curve maximizes the dilution index. The ratio between observed and maximum dilution index is denoted reactor ratio. For a 300-compartment solute sampler, covering an area of 0.75 m², we compute a reactor ratio of 0.665, compared with 0.04 for stochastic-convective and 1 for convective-dispersive transport. With a single, large collector the reactor ratio would be 0.958, severely underestimating concentration variations. Large collector areas are clearly inadequate to estimate dilution. Values of the dilution index and the reactor ratio for individual sampling compartments indicate efficient longitudinal mixing in most but not all cases, and considerable spatial variation of the leaching process.

Drying and denaturation characteristics of α-lactalbumin, β-lactoglobulin, and bovine serum albumin in a convective drying process

Drying and denaturation kinetics of aqueous droplets of α-lactalbumin (α-lac), β-lactoglobulin (β-lg), and bovine serum albumin (BSA) were measured in a convective drying environment. Single droplets having an initial droplet diameter of 2 ± 0.1 mm and containing 10% (w/v) protein concentration were dried using conditioned air (65 and 80 °C, 2-3% RH, 0.5 m/s velocity) for 600 s. The denaturation of these proteins was measured by using reversed-phase HPLC. At the end of 600 s of drying 13.3 and 19.4% α-lac was found to be lost due to denaturation at 65 and 80 °C, respectively. Up to 31.0% of β-lg was found to be denatured, whereas BSA was not found to be significantly (p > 0.05) denatured in these drying conditions. The formation and strength of skin and the associated morphological features were found to be linked with the degree of denaturation of these proteins. The secondary structure of these proteins was significantly (p < 0.05) affected and altered by the drying stresses. The β-sheet and random coil contents were increased in α-lac by 6.5 and 4.0%, respectively, whereas the α-helix and β-turn contents decreased by 5.5 and 5.0%, respectively. The β-sheet and random coil contents in β-lg were increased by 7.5 and 2.0%, respectively, whereas the α-helix and β-turn contents decreased by 3.5 and 6.0%, respectively. In the case of BSA the β-sheet, α-helix, and random coil contents were found to increase, whereas the β-turn content decreased.