Proteins and protein-rich biomass as environmentally friendly adsorbents selective for precious metal ions.

Proteins exhibit specific interactions with various metal ions, which play important roles in a living cell. Here, we found that various proteins selectively adsorbed precious metal ions at a wide range of pH values. Studies on protein sequences and on synthesized peptides revealed that a histidine-containing sequence had specific interactions with precious metal ions (Au3+ and Pd2+).

Inhibitiory effects of gold(III) ions on ribonuclease and deoxyribonuclease.

Inhibitory effects of gold(III) ions (Au(III)) on ribonuclease A (RNase A) and deoxyribonuclease I (DNase I) were investigated at neutral pH. RNase A was completely inhibited by 3 molar equivalents of Au(III) ions. DNase I was inhibited by 10 molar equivalents of Au(III) ions.

Liquid membrane operations in a microfluidic device for selective separation of metal ions.

A three-phase flow, water/n-heptane/water, was constructed in a microchannel (100-microm width, 25-microm depth) on a glass microchip (3 cm x 7 cm) and was used as a liquid membrane for separation of metal ions. Surface modification of the microchannel by octadecylsilane groups induced spontaneous phase separation of the three-phase flow in the microfluidic device, which allows control of interfacial contact time and off-chip analysis using conventional analytical apparatus. Prior to the selective transport of a metal ion through the liquid membrane in the microchannel, the forward and backward extraction of yttrium and zinc ions was investigated in a two-phase flow on a microfluidic device using 2-ethylhexyl phosphonic acid mono-2-ethylhexyl ester (commercial name, PC-88A) as an extractant.