• Journal of the Korean Chemical Society
• /
• v.50 no.3
• /
• pp.224-231
• /
• 2006

agents used for enhancing mechanical properties of porous natural scaffolds, reduces biocompatability of the scaffolds, due to their inherent cytotoxicity. In this study, scaffolds which was composed of chitosan, alginate and gelatin were cross-linked by using heat treatment instead of cross-linking agent and mechanical properties of the cross-linked scaffold were investigated. Fourier transform infrared spectroscopy (FT-IR) analysis confirmed that cross-linking of heat-treated scaffold was formed via amide or ester linkage between the polymer chains. The heat-treated scaffold had interconnected pores with mean diameter of 100~200 m and showed more than two fold increase of water uptake in comparison with chemically cross-linked scaffold. Tensile strength of the heat-treated scaffold increased up to 130% compared to non cross-linked scaffold and average maximum elongation was 11.3%. The porous cross-linked scaffold with the improved mechanical property may be suitable as a biocompatable scaffold for tissue engineering.

• BMB Reports
• /
• v.33 no.2
• /
• pp.133-137
• /
• 2000

To elucidate the effect of oxygen radicals on the molecular properties of proteins, the secondary and tertiary structure and molecular weight size of BSA and ${\beta}$-lactoglobulin were examined after irradiation of proteins at various doses. Gamma-irradiation of protein solutions caused the disruption of the ordered structure of protein molecules as well as degradation, cross-linking, and aggregation of the polypeptide chains. As a model system, BSA and ${\beta}$-lactoglobulin were used as a typical ${\alpha}$-helical and a ${\beta}$-sheet structure protein, respectively. A circular dichroism study showed that the increase of radiation decreased the ordered structure of proteins with a concurrent increase of aperiodic structure content. Fluorescence spectroscopy indicated that irradiation quenched the emission intensity excited at 280 nm. SDS-PAGE and a gel permeation chromatography study indicated that radiation caused initial fragmentation of proteins resulting in a subsequent aggregation due to cross-linking of protein molecules.

• Journal of Microbiology and Biotechnology
• /
• v.8 no.4
• /
• pp.416-421
• /
• 1998

A carboxyl group modifier, l-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) was used to study the interactions between three components of toluene dioxygenase (TDO) from Pseudomonas putida FI. $Ferredoxin_{TOL}$ activity was increased by the treatment with EDC; however, the activity was rapidly declined in the prolonged incubation. In covalent cross-linking experiments with EDC, $Ferredoxin_{TOL}$ made a one-to-one complex with $Reductase_{TOL}$ or the large subunit of $ISP_{TOL}$. These results provide evidence for the involvement of electrostatic interactions in the TDO electron transfer system.

• BMB Reports
• /
• v.35 no.6
• /
• pp.590-594
• /
• 2002

To elucidate the effect of gamma-irradiation on the molecular properties of myoglobin, the secondary and tertiary structures, as well as the molecular weight size of the protein, were examined after irradiation at various irradiation doses. Gamma-irradiation of myoglobin solutions caused the disruption of the ordered structure of the protein molecules, as well as degradation, cross-linking, and aggregation of the polypeptide chains. A SDS-PAGE study indicated that irradiation caused initial fragmentation of the proteins and subsequent aggregation, due to cross-linking of the protein molecules. The effect of irradiation on the protein was more significant at lower protein concentrations. Ascorbic acid protected against the degradation and aggregation of proteins by scavenging oxygen radicals that are produced by irradiation. A circular dichroism study showed that an increase of the irradiation decreased the a-helical content of myoglobin with a concurrent increase of the aperiodic structure content. Fluorescence spectroscopy indicated that irradiation increased the emission intensity that was excited at 280 nm.

• Applied Chemistry for Engineering
• /
• v.30 no.6
• /
• pp.643-651
• /
• 2019

Polybenzimidazole (PBI), an engineering polymer with well-known excellent thermal, chemical and mechanical stabilities has been recognized as an alternative to high temperature polymer electrolyte membranes (HT-PEMs). This review focuses on recent advances made on the development of PBI-based HT-PEMs for fuel cell applications. PBI-based membranes discussed were prepared by various strategies such as structural modification, cross-linking, blending and organic-inorganic composites. In addition, intriguing properties of the PBI-based membranes as well as their fuel cell performances were highligted.

• Proceedings of the KIEE Conference
• /
• 2015.07a
• /
• pp.1130-1131
• /
• 2015

팰릿 형태의 XLPE (Cross-Linking Polyethylene)를 Hot Press로 시험편을 제작하여 열분석 데이터 처리장치를 이용하여 시차 주사 열량법 (differential scanning calorimetry, DSC)과 열 중량 분석 (Thermo gravimetric analysis, TGA) 등으로 열적 특성을 분석하였다. 분석 결과, XLPE의 전이온도 피크는 $61^{\circ}C$, 용융온도에 해당하는 피크는 $102^{\circ}C$에서 나타났으며 XLPE의 TG 분석 결과 $470^{\circ}C$ 근처에서 한 번의 급격한 열중량 감소를 보였으며 $800^{\circ}C$까지 측정 후 잔류물은 완전 분해되어 거의 존재하지 않았음을 알 수 있었다.

• Food Science and Biotechnology
• /
• v.14 no.1
• /
• pp.16-20
• /
• 2005

Additions of ground garlic, chili and ginseng powder did not affect the breaking force and strain of directly heated gel of Alaska pollack surimi. In comparison, these additives reduced the setting effect achieved by incubation of the salted surimi at $25^{\circ}C$, and resulted in a decreased breaking force and strain for the two step heated gel. Garlic almost completely inhibited the myosin cross-linking reaction, an important reaction for improving the gel properties occurring in the setting process. However, chili and ginseng powder minimally inhibited the cross-linking reaction. Thus, this study proposes that the mechanism for the suppression of the setting effect by chili and ginseng is different from that of garlic.

• Transactions on Electrical and Electronic Materials
• /
• v.11 no.2
• /
• pp.69-72
• /
• 2010

This study investigates the thermal and mechanical properties of insulation elements through the mixing of epoxy based micro and nano particles. Regarding their thermal properties, differential scanning calorimeter and dynamic mechanical analyser were used to calculate the cross-linking densities for various types of insulation elements. The mechanical properties of the bending strength, the shape and scale parameters, were obtained using the Weibull plot. This study obtained the best results in the scale parameters, at 0.5 phr, for the bending strength of the epoxy nano-and-micro mixture composites.

• Restorative Dentistry and Endodontics
• /
• v.37 no.1
• /
• pp.2-8
• /
• 2012

The limited durability of resin-dentin bonds severely compromises the longevity of composite resin restorations. Resin-dentin bond degradation might occur via degradation of water-rich and resin sparse collagen matrices by host-derived matrix metalloproteinases (MMPs). This review article provides overview of current knowledge of the role of MMPs in dentin matrix degradation and four experimental strategies for extending the longevity of resin-dentin bonds. They include: (1) the use of broadspectrum inhibitors of MMPs, (2) the use of cross-linking agents for silencing the activities of MMPs, (3) ethanol wet-bonding with hydrophobic resin, (4) biomimetic remineralization of water-filled collagen matrix. A combination of these strategies will be able to overcome the limitations in resin-dentin adhesion.

• Proceedings of the Korean Society of Postharvest Science and Technology of Agricultural Products Conference
• /
• 2003.10a
• /
• pp.135.1-135
• /
• 2003

To elucidate the effect of gamma-irradiation on the molecular properties of hemoglobin, the secondary, tertiary structure, and the molecular weight size of the protein were examined after irradiation at 0.5, 1, 5, and 10 kGy. Gamma-irradiation of hemoglobin solutions caused the disruption of the ordered structure of the protein molecules, as well as degradation, cross-linking, and aggregation of the polypeptide chains. A SDS-PAGE study indicated that irradiation caused initial fragmentation of the proteins and subsequent aggregation due to cross-linking of the protein molecules. The effect of irradiation on the protein was more significant at lower protein concentrations. Ascorbic acid decreased the degradation and aggregation of proteins by scavenging oxygen radicals that were produced by irradiation. A circular dichroism study showed that irradiation decreased the helical content of hemoglobin with a concurrent increase of the aperiodic structure content. Fluorescence spectroscopy indicated that irradiation decreased the emission intensity that was excited at 280 nm.