Background: Biocatalytic processes often require a full recycling of biocatalysts to optimize economic benefits and minimize waste disposal. Immobilization of biocatalysts onto particulate carriers has been widely explored as an option to meet these requirements. However, surface properties often affect the amount of biocatalysts immobilized, their bioactivity and stability, hampering their wide applications. The aim of this work is to explore how immobilization of lipases onto magnetite nanoparticles affects their biocatalytic performance under carefully controlled surface modification. Methodology/Principal Findings: Magnetite nanoparticles, prepared through a co-precipitation method, were coated with alkyl silanes of different alkyl chain lengths to modulate their surface hydrophobicity. Candida rugosa lipase was then directly immobilized onto the modified nanoparticles through hydrophobic interaction. Enzyme activity was assessed by catalytic hydrolysis of p-nitrophenyl acetate. The activity of immobilized lipases was found to increase with increasing chain length of the alkyl silane. Furthermore, the catalytic activities of lipases immobilized on trimethoxyl octadecyl silane (C18) modified Fe3O4 were a factor of 2 or more than the values reported from other surface immobilized systems. After 7 recycles, the activities of the lipases immobilized on C18 modified nanoparticles retained 65%, indicating significant enhancement of stability as well through hydrophobic interaction. Lipase immobilized magnetic nanoparticles facilitated easy separation and recycling with high activity retaining. Conclusions/Significance: The activity of immobilized lipases increased with increasing alkyl chain length of the alkyl trimethoxy silanes used in the surface modification of magnetite nanoparticles. Lipase stability was also improved through hydrophobic interaction. Alkyl silane modified magnetite nanoparticles are thus highly attractive carriers for enzyme immobilization enabling efficient enzyme recovery and recycling.

Spherical assemblies with core/shell configurations are prepared through C-terminal amidated short peptide mediated self-association of platinum nanocrystals. The interactions between the peptides might drive the self-assembly of platinum nanocrystals and determine their surface properties. Thus, the nanosize assemblies collapse and spread on a hydrophilic surface, whereas maintaining their spherical shapes on a hydrophobic surface.

As a major constituent of egg white matrix, ovalbumin has long been perceived to be implicated in the formation of avian eggshells, in particular, the mammillary layer. However, very little is known about the detailed mechanism by which this protein mediates shell calcification. By the combined studies of AFM, SEM, and TEM, we have investigated the influence of ovalbumin on CaCO(3) precipitation under in vitro mineralization conditions. We observed that the influence was multifold. This protein modified the morphology of calcite crystals through a distinct anisotropic process with respect to the four crystal step edges. AFM characterization revealed that the modification was initiated at the obtuse-obtuse step corner and propagated predominantly along the obtuse steps. Furthermore, the protein favored the existence of unstable phases such as amorphous calcium carbonate and crystalline vaterite. In contrast, lysozyme, another protein also present in the system, played a very different role in modifying calcite morphology. The mechanistic understanding gained from this study is clearly also of practical significance in developing advanced inorganic CaCO(3) materials with the aid of morphological manipulation of crystalline structures via different protein mediation.

Peptide self-assembly is a hierarchical process, often starting with the formation of alpha-helices, beta-sheets or beta-hairpins. However, how the secondary structures undergo further assembly to form higher-order architectures remains largely unexplored. The polar zipper originally proposed by Perutz is formed between neighboring beta-strands of poly-glutamine via their side-chain hydrogen bonding and helps to stabilize the sheet. By rational design of short amphiphilic peptides and their self-assembly, here we demonstrate the formation of polar zippers between neighboring beta-sheets rather than between beta-strands within a sheet, which in turn intermesh the beta-sheets into wide and flat ribbons. Such a super-secondary structural template based on well-defined hydrogen bonds could offer an agile route for the construction of distinctive nanostructures and nanomaterials beyond beta-sheets.=20

The adsorption of a series of cationic lipopeptide surfactants, C14Kn (where C14 denotes the myristic acyl chain and Kn represents n number of lysine residues) at the hydrophobic solid/water interface has been studied using spectroscopic ellipsometry (SE) and neutron reflection (NR). The hydrophobic C8 surface was prepared by grafting a monolayer of octyltrimethoxysilane on the silicon surface. SE was used to follow the dynamic adsorption from these lipopeptide surfactants and the amount was found to undergo a fast increase within the first 2-3 min, followed by a much slower process tending to equilibration in the subsequent 15-20 min. Lipopetide surfactants with n =3D 1-4 showed similar dynamic features, indicating that the interaction between the acyl chain and the C8 surface is the main driving force for adsorption. The saturation adsorption amount of C14Kn at the C8/water interface was found to be inversely related to the increasing number of Lys residues in the head group due to the increase of steric hindrance and electrostatic repulsion between the head groups. Solution concentration had a significant effect on the initial adsorption rate, similar to the feature observed from nonionic surfactants CmEn. The structure of the adsorbed layers was studied by NR in conjunction with isotopic contrasts. The layer formed by the head groups of C14K1 was 10 A thick, and those formed by C14K2, C14K3 and C14K4 head groups were all about 13 A thick. In contrast, the thicknesses of the layers formed by hydrophobic tails of C14K1, C14K2 C14K3, and C14K4 were found to be 17, 13, 10, and 10 A, respectively, resulting in the steady increase of area per molecule at the interface from 29 =C2=B1 2 A(2) for C14K1 to 65 =C2=B1 2 A(2) for C14K4. Thus, with an increase in the head group length, the molecules in the adsorbed layer tended to lie down upon adsorption. =20

To improve the stability of foam fluids, SiO2 nanoparticles and trace amount of Gemini cationic surfactant were combined with the main foaming agent, nonionic surfactant, to form a tricomponent multiphase foam. The stability of the multiphase foam was assessed through two parameters of half-life time and dilational modulus. The Interaction between surfactants and nanoparticles were studied though surface tension, adsorption amount, and C potential measurement. The effects of saline ions and temperature on foam stability were also investigated. The plugging ability of the tricomponent multiphase foam was assessed using a sandpack model. The optimized tricomponent multiphase foam was 10 times more stable than corresponding foam without nanoparticles in terms of half-life time and also resisted to saline and temperature to a certain degree because the adsorption of nanoparticles at the interface improved the mechanic strength of foam film. The tricomponent multiphase foam showed more excellent plugging ability in porous media than foam without nanoparticles during flooding. The adsorption of cationic surfactant not only changed the surface hydrophobicity of the SiO2 nanoparticles, but also promoted the adsorption of APG molecules. Combined the results of Gemini C12C3C12Br2 replaced by CTAB or SDS, and C12C3C12Br2/SiO2 replaced by pretreated partially hydrophobic SiO2 nanoparticle (H15), it is deduced that the in situ surface modification by cationic adsorption to a suitable hydrophobicity was a key step in multiphase stability. Compared with the pretreated partially hydrophobic SiO2 nanoparticle, more SiO2 nanoparticles were distributed at the air/liquid interface and utilized effectively in the tricomponent multiphase foam.

It is difficult to maintain a target membrane protein in a soluble and functional form in aqueous solution without biological membranes. Use of surfactants can improve solubility, but it remains challenging to identify adequate surfactants that can improve solubility without damaging their native structures and biological functions. Here we report the use of a new class of lipopeptides to solubilize photosystem I (PS-I), a well known membrane protein complex. Changes in the molecular structure of these surfactants affected their amphiphilicity and the goal of this work was to exploit a delicate balance between detergency and biomimetic performance in PS-I solubilization via their binding capacity. Meanwhile, the effects of these surfactants on the thermal and structural stability and functionality of PS-I in aqueous solution were investigated by circular dichroism, fluorescence spectroscopy, SDS-PAGE analysis and O-2 uptake measurements, respectively. Our studies showed that the solubility of PS-I depended on both the polarity and charge in the hydrophilic head of the lipopeptides and the length of its hydrophobic tail. The best performing lipopeptides in favour of PS-I solubility turned out to be C14DK and C16DK, which were comparable to the optimal amphiphilicity of the conventional chemical surfactants tested. Lipopeptides showed obvious advantages in enhancing PS-I thermostability over sugar surfactant DDM and some full peptide amphiphiles reported previously. Fluorescence spectroscopy along with SDS-PAGE analysis demonstrated that lipopeptides did not undermine the polypeptide composition and conformation of PS-I after solubilization; instead they showed better performance in improving the structural stability and integrity of this multi-subunit membrane protein than conventional detergents. Furthermore, O-2 uptake measurements indicated that PS-I solubilized with lipopeptides maintained its functionality. The underlying mechanism for the favorable actions of lipopeptide in PS-I solubilization and stabilization is discussed.