Surface functionalization of chitosan as a coating material for orthopaedic applications: A comprehensive review.

Metallic implants have dominated the biomedical implant industries for the past century for load-bearing applications, while the polymeric implants have shown great promise for tissue engineering applications. The surface properties of such implants are critical as the interaction of implant surfaces, and the body tissues may lead to unfavourable reactions. Desired implant properties are biocompatibility, corrosion resistance, and antibacterial activity. A polymer coating is an efficient and economical way to produce such surfaces. A lot of research has been carried out on chitosan (CS)-modified metallic and polymer scaffolds in the last decade. Different methods such as electrophoretic deposition, sol-gel methods, dip coating and spin coating, electrospinning, etc. have been utilized to produce CS coatings. However, a systematic review of chitosan coatings on scaffolds focussing on widely employed techniques is lacking. This review surveys literature concerning the current status of orthopaedic applications of CS for the purpose of coatings. In this review, the various preparation methods of coating, and the role of the surface functionalities in determining the efficiency of coatings are discussed. Effect of nanoparticle additions on the polymeric interfaces and in regulating the properties of surface coatings are also investigated in detail.

Nitrilase-catalysed conversion of acrylonitrile by free and immobilized cells of Streptomyces sp.

The biotransformation of acrylonitrile was investigated using thermophilic nitrilase produced from a new isolate Streptomyces sp. MTCC 7546 in both the free and immobilized state. Under optimal conditions,the enzyme converts nitriles to acids without the formation of amides.The whole cells of the isolate were immobilized in agar-agar and the beads so formed were evaluated for 25 cycles at 50 degrees C. The enzyme showed a little loss of activity during reuse. Seventy-one per cent of 0.5 M acrylonitrile was converted to acid at 6 h of incubation at a very low density of immobilized cells, while 100% conversion was observed at 3 h by free cells.

Biobleaching of nonwoody pulps using xylanase of Bacillus brevis BISR-062.

The efficiency of xylanase of Bacillus brevis BISR-062 as a prebleaching agent was evaluated on three nonwoody pulps at two different pH values (7.0 and 8.5). Crude xylanase was found to have an optimum temperature and pH of 65-70 degrees C and 7.0, respectively. The stability of the enzyme was determined at two pH values (7.0 and 8.0), and it lost approx 50% of its activity at both values within 2 h at 50 degrees C. However, the enzyme was found to be effective as a prebleaching agent only with rice straw pulp. A maximum brightness gain of 6 points was obtained with this pulp at pH 7.0. The strength properties of the rice straw pulp at pH 7.0 also improved as the result of enzyme treatment.

Inhibition of protein prenylation by metabolites of limonene.

The monoterpenes limonene and perillyl alcohol are undergoing clinical evaluation in cancer patients. In this paper, we report the chemical synthesis, characterisation, and quantitation in patients' plasma of a novel human metabolite of limonene, which is identified as an isomer of perillic acid. The synthesis of R-perillic acid is also described, because previous reports on the activity of perillic acid against isoprenylation enzymes refer to the S-enantiomer, although it is the R-enantiomer which is the metabolite of R-limonene. The above monoterpenes, with several related compounds, were assayed for inhibitory activity towards the isoprenylation enzymes in rat brain cytosol. Although R- and S-limonene are only weak inhibitors of the isoprenylation enzymes, their major metabolites, perillic acid and perillyl alcohol, are more potent inhibitors, with IC50 values in the low mM range. The metabolites possess greater activity towards the geranylgeranyltransferase type I enzyme than farnesyltransferase, while the novel metabolite displays IC50 values similar to those of perillic acid suggesting that it may contribute to the in vivo activity of limonene.