• Applied Chemistry for Engineering
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• v.26 no.2
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• pp.199-204
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• 2015

Thermoplastic road markings are one of the most widely used road markings in the world. However, the durability of domestic road markings is relatively shorter than that of the global average of, approximately, three years. To overcome it, the conventional thermoplastic road markings were prepared by adding polyolefin and oxidized PE wax to conventional petroleum resin. In addition, the melting viscosity was designed below 500 cP at $220^{\circ}C$ as well as the optimum viscosity for spray painting, and embedding ratio of glass beads were controlled about 50~60% by spraying in an interval of 1 second. Also the glass bead adhesive ratio was improved by reducing the amount of $CaCO_3$ below 40 wt%. The retroreflectivity was tested under four different conditions to evaluate the abrasion resistance of thermoplastic road markings. The retroreflectivity coefficient satisfied the international standard ($150mcd{\cdot}m^{-2}{\cdot}lux^{-1}$) in this study, and TPRM-7 was determined as an optimal ratio.

• KSBB Journal
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• v.21 no.4
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• pp.279-285
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• 2006

We investigated the effects of immobilization chemistry on the yield of immobilization and the bioactivity of the immobilized enzymes. Trypsin as a model protein and macroporous polymer beads(Toyopearl AF 650M, Tosho Co., Japan) was used as a model matrix. Four methods were used to immobilize trypsin; covalent conjugation by reductive amination(at pH 10.0 and pH 4.0) and affinity interaction via streptavidin-biotin, and double-affinity interaction via biotin-streptavidin-biotin system. The covalent conjugation immobilized $3{\sim}4$ mg/ml-gel, ca. 3-fold higher than the affinity method. However, the specific activity of the covalently(pH 10.0) and affinity-immobilized trypsin(via streptavidin-biotin) are ca. 37% and 50%, respectively, of that of the soluble enzyme(on the low-molecular-weight BAPNA substrate). When the molecular size of a substrate increased, the affinity-immobilized trypsin showed higher clavage activity on insulin and BSA. This result seemed to indicate the streptavidin-biotin system allowed more steric flexibility of the immobilized trypsin in its interaction with a substrate molecule. To confirm this, we studied the molecular flexibility of immobilized trypsin using quartz crystal microbalance-dissipation. Self-assembled monolayers were formed on the Q-sensor surface by aminoalkanethiols, and gultaraldehyde was attached to the SAMs. Trypsin was immobilized in two ways: reductive amination(at pH 10.0) and the streptavidin-biotin system. The dissipation shift of the affinity-immobilized trypsin was $0.8{\times}10^{-6}$, whereas that of the covalently attached enzyme was almost zero. This result confirmed that the streptavidin-biotin system allowed higher molecular flexibility. These results suggested that the bioactivity of the immobilized enzyme be strongly dependent on its molecular flexibility.