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Subtle changes in the monolayer structure of nanoparticles (NPs) influence the interfacial behavior of both NPs and NP-protein conjugates. In this study, we use a series of monolayer-protected gold NPs to explore the role of particle hydrophobicity on their dynamic behavior at the toluene-water interface. Using dynamic surface tension measurements, we observed a linear decrease in the meso-equilibrium surface tension (γ) and faster dynamics as the hydrophobicity of the ligands increases. Further modulation of γ is observed for the corresponding NP-protein complexes at the charge-neutralization point.

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An endo-beta-1,4-glucanase from a thermoacidophilic fungus, Aspergillus terreus M11, was purified 18-fold with 14% yield and a specific activity of 67 U mg(-1) protein. The optimal pH was 2 and the cellulase was stable from pH 2 to 5. The cellulase had a temperature optimum of 60 degrees C measured over 30 min and retained more than 60% of its activity after heating at 70 degrees C for 1 h. The molecular mass of the cellulase was about 25 kDa. Its activity was inhibited by 77% by Hg(2+) (2 mM) and by 59% by Cu(2+) (2 mM).