Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Biopolymer behavior

In this section, we review the statistical mechanical approach to the problem of the folding of long polymer chains. From the standpoint of physics, considerable efforts have been made to extract simple and universal laws of biopolymers behavior regardless of their complexity and diversity. This leads... [Pg.42]

Horne, D.S. and Patino, J.M.R. Adsorbed biopolymers behavior in food applications. Biopolymers at Interfaces, 2nd Ed., M. Malmsten, ed., Marcel Dekker, New York, 2003, chap. 30. [Pg.271]

Chirooptical properties give more subtle information on the conformational behavior of biopolymers and peptides in solution. In early experiments, optical rotation and optical rotatory dispersion (ORD) have been recognized as valuable techniques, followed more recently by significant progress and refinements in the equipment which have resulted in the routine measurements of applied circular dichroism (CD). [Pg.162]

The results of mechanical properties (presented later in this section) showed that up to 20 phr, the biofillers showed superior strength and elongation behavior than CB, cellulose being the best. After 30 phr the mechanical properties of biocomposites deteriorated because of the poor compatibility of hydrophilic biopolymers with hydrophobic natural rubber(results not shown). While increasing quantity of CB in composites leads to constant increase in the mechanical properties. Scanning electron micrographs revealed presence of polymer-filler adhesion in case of biocomposites at 20 phr. [Pg.122]

The first elastomeric protein is elastin, this structural protein is one of the main components of the extracellular matrix, which provides stmctural integrity to the tissues and organs of the body. This highly crosslinked and therefore insoluble protein is the essential element of elastic fibers, which induce elasticity to tissue of lung, skin, and arteries. In these fibers, elastin forms the internal core, which is interspersed with microfibrils [1,2]. Not only this biopolymer but also its precursor material, tropoelastin, have inspired materials scientists for many years. The most interesting characteristic of the precursor is its ability to self-assemble under physiological conditions, thereby demonstrating a lower critical solution temperature (LCST) behavior. This specific property has led to the development of a new class of synthetic polypeptides that mimic elastin in its composition and are therefore also known as elastin-like polypeptides (ELPs). [Pg.72]

The coacervation of tropoelastin plays a crucial role in the assembly into elastic fibers. This coacervation is based on the LCST behavior of tropoelastin, which causes tropoelastins structure to become ordered upon raising the temperature. The loss of entropy of the biopolymer is compensated by the release of water from its chain [2, 18, 19]. This release of water results in dehydration of the hydrophobic side chains, and this is the onset of the self-assembly leading to the alignment of tropoelastin molecules. [Pg.77]

After expression of poly(VPGXG) genes, the biopolymer can easily be purified from a cellular lysate via a simple centrifugation procedure, because of the inverse temperature transition behavior. This causes the ELPs to undergo a reversible phase transition from being soluble to insoluble upon raising the temperature above the and then back to soluble by lowering the temperature below Tt (Fig. 9). The insoluble form can be induced via addition of salt [27]. The inverse transition can... [Pg.80]

Teeuu, D. and Hesselink, F.T. "Power-Law Flow and Hydrodynamic Behavior of Biopolymer Solutions In Porous Media," SPE paper 8982, 1980 SPE Fifth International Symposium on Oilfield and Geothermal Chemistry, Stanford, May 28 30. [Pg.661]

It did not give rise to phase separation or precipitation. Similar behavior was observed when other types of polysaccharides were examined [53,54]. By now all the commercially important polysaccharides have been applied to the fabrication of hybrid silica nanocomposites in accordance with Scheme 3.2. What is more, various proteins have been entrapped in silica by the same means. In all instances the THEOS demonstrated good biocompatibility with biopolymers, even though its amount in formulations was sometimes up to 60 wt%. Biopolymer solutions after the precursor admixing remained homogeneous to the point of transition into a gel state. [Pg.89]

In this chapter, immobilization of proteins on these mesoporous silicas and PMO is first introduced, followed by a description of protein immobilization on mesoporous carbon materials. The adsorption behavior of other biopolymers such as... [Pg.115]

Nucleic acids, DNA and RNA, are attractive biopolymers that can be used for biomedical applications [175,176], nanostructure fabrication [177,178], computing [179,180], and materials for electron-conduction [181,182]. Immobilization of DNA and RNA in well-defined nanostructures would be one of the most unique subjects in current nanotechnology. Unfortunately, a silica surface cannot usually adsorb duplex DNA in aqueous solution due to the electrostatic repulsion between the silica surface and polyanionic DNA. However, Fujiwara et al. recently found that duplex DNA in protonated phosphoric acid form can adsorb on mesoporous silicates, even in low-salt aqueous solution [183]. The DNA adsorption behavior depended much on the pore size of the mesoporous silica. Plausible models of DNA accommodation in mesopore silica channels are depicted in Figure 4.20. Inclusion of duplex DNA in mesoporous silicates with larger pores, around 3.8 nm diameter, would be accompanied by the formation of four water monolayers on the silica surface of the mesoporous inner channel (Figure 4.20A), where sufficient quantities of Si—OH groups remained after solvent extraction of the template (not by calcination). [Pg.134]

Defeijter, J. A. Benjamins, J. Veer, F. A., Ellipsometry as a tool to study adsorption behavior of synthetic and biopolymers at air water interface, Biopolymers 1978, 17, 1759 1772... [Pg.294]


See other pages where Biopolymer behavior is mentioned: [Pg.121]    [Pg.121]    [Pg.584]    [Pg.157]    [Pg.166]    [Pg.192]    [Pg.257]    [Pg.556]    [Pg.169]    [Pg.461]    [Pg.7]    [Pg.87]    [Pg.124]    [Pg.86]    [Pg.81]    [Pg.86]    [Pg.216]    [Pg.220]    [Pg.203]    [Pg.200]    [Pg.12]    [Pg.12]    [Pg.669]    [Pg.244]    [Pg.244]    [Pg.6]    [Pg.15]    [Pg.17]    [Pg.18]    [Pg.23]    [Pg.10]    [Pg.18]    [Pg.128]    [Pg.200]    [Pg.407]    [Pg.209]    [Pg.70]    [Pg.72]    [Pg.302]   
See also in sourсe #XX -- [ Pg.65 ]




SEARCH



© 2024 chempedia.info