• Journal of the Korean Wood Science and Technology
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• v.45 no.5
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• pp.599-612
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• 2017

Human hair (HH) is produced as a waste from beauty parlor and barbershop. HH-based adhesives were formulated with NaOH-hydrolyzed HH, $H_2SO_4$-hydrolyzed chicken blood (CB) and PF as a crosslinking agent. Physicochemical properties and retention rate against hot water of the adhesives were measured to investigate the potential of HH as a raw material of wood adhesives. HH was composed of keratin-type protein of 80% and over. Ash of less than 0.1% was contained in HH. Among the amino acids included in HH, glutamic acid showed the highest content, followed by cysteine, serine, arginine and threonine. Solid content of the adhesives ranged from 33.2% to 41.8% depending on hydrolysis conditions of HH and PF type. Viscosity at $25^{\circ}C$ ranged from 300 to $600mPa{\cdot}s$ resulting in a sprayable adhesive. Retention rate against hot water measured to evaluate the water resistance of adhesives was the highest in the cured resin formulated with 5% NaOH-hydrolyzed HH and 5% $H_2SO_4$-hydrolyzed CB. Meanwhile, the molar ratio of formaldehyde to phenol in PF did not have a significant impact on the retention rate of HH-based adhesives. When the retention rates of HH-based adhesives were compared to those of conventional wood adhesive resins used for the production of wood-based panels extensively, HH-based adhesives formulated with 30 wt% PF showed lower retention rate than commercial urea-formaldehyde resin. However, when PF content was increased to 35 wt%, the retention rate greatly increased and approached to that of commercial melamine-urea-formaldehyde resin. Except for the results mentioned above, the analysis of economic feasibility suggests that HH-based adhesives can be used for the production of wood-based panels if HH is hydrolyzed in proper conditions and then the HH-based adhesives are formulated by the HH hydrolyzates with 35 wt% PF.

• Journal of Environmental Science International
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• v.23 no.6
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• pp.1095-1100
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• 2014

Keratin wastes are generated in excess of million tons per year worldwide and biodegradation of keratin by microorganisms possessing keratinase activity can be used as an alternative tool to prevent environmental pollution. For practical use of keratinase, its physicochemical properties should be investigated in detail. In this study, we investigated characteristics of keratinase produced by Xanthomonas sp. P5 which is isolated from rhizospheric soil of soybean. The level of keratinase produced by the strain P5 increased with time and reached its maximum (10.6 U/ml) at 3 days. The production of soluble protein had the same tendency as the production of keratinase. Optimal temperature and pH of keratinase were $40^{\circ}C-45^{\circ}C$ and pH 9, respectively. The enzyme showed broad temperature and pH stabilities. Thermostability profile showed that the enzyme retained 94.6%-100% of the original activity after 1 h treatment at $10^{\circ}C-40^{\circ}C$. After treatment for 1 h at pH 6-10, 89.2%-100% of the activity was remained. At pH 11, 71.6% of the original activity was retained after 1 h treatment. Although the strain P5 did not degrade human hair, it degraded duck feather and chicken feather. These results indicate that keratinase from Xanthomonas sp. P5 could be not only used to upgrade the nutritional value of feather hydrolysate but also useful in situ biodegradation of feather.