• Journal of the Korean Society of Clothing and Textiles
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• v.41 no.2
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• pp.341-351
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• 2017

This study evaluates a cleaning method to maintain and minimize the change of blood soil for the selective removal of stains from textiles with historical significance and special meaning. Cotton and silk fabrics were soiled with blood, aged artificially and then washed by wet cleaning or dry cleaning (water, nonionic surfactant; Triton, natural surfactant; saponin, organic solvent; n-Decane). The washed fabrics were stored at room temperature for four years. The change of the blood soil was evaluated by SEM, weight, thickness, and color differences. Subsequently, the shape and the amount of blood adsorption on the fabric varied depending on fiber type and fabric structure characteristics; in addition, long term storage affected changes to blood soil. It was difficult to remove artificially aged blood soil from fabrics by wet or dry cleaning. However, the changes of the blood soil by these cleanings can be explained by the changes on SEM, weight, thickness and fabric color. The changes (especially color) showed over time. Wet cleaning showed that the changes of those factors were slightly lower than those by dry cleaning.

• Fashion & Textile Research Journal
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• v.22 no.4
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• pp.534-539
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• 2020

Experimental research is needed to provide information on the removal of bloodstains since washing clothes contaminated with blood is necessary for medical related fields (such as ambulance workers and doctors) as well as for women of childbearing age. This study investigated efficient washing conditions for the removal of bloodstains with a focus on washing temperature, fiber type and blood ageing time. Polyester/cotton fabric showed the highest detergency from among three fabrics that were influenced by the composition of the fiber and the structure of the yarn and fabric. When examining the effect of detergent, it was concluded that the alkalinity over pH 10 was essential to remove bloodstains and that auxiliary agents such as soil antiredeposition agents and bleach had a significant effect on the removal of bloodstains. Washing temperature showed the highest detergency at 20℃ due to the activity of the enzyme without the denaturalization of blood. Blood-ageing influenced detergency by inducing changes in the adsorption area and chemical bond. A combination of methods such as quick removal after contamination, use of alkaline detergents including soil antiredeposition agents and bleach, and low-temperature washing could help remove bloodstains.

• Journal of the Korean Society of Clothing and Textiles
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• v.20 no.4
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• pp.655-666
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• 1996

The effect of protease (subtilisin Carlsberg) on the removal of hemoglobin as protein soil was studied. The relation between the renloval and the hydrolysis of hemoglobin by subtilisin Carlsberg was discussed. The soiled babric was prepared by spotting of hemoglobin solution evenly on the cotton fabric and was denatured by steaming. The soiled fabric was washed by using Terg-0-Tometer at various conditions. The removal efficiency was evaluated by analysis of protein on the fabrics before and after washing by means of copper-Folin method. 1. The removal of hemoglobin was increased in proportion to increasing of the enzyme concentration up to a certain point, but it began to decrease above the point. 2. The hemoglobin was removed effectively by adding of subtilisin Carlsberg, and more effectively removed by adding of AOS in the enzyme solution. 3. The removal of hemoglobin deviated from the first order reaction in detergency. 4. The renloval of hemoglobin was highest at $50^{\circ}C$ in detergency, Even at low temperature the removal efficiency of enzyme was relatively higher compared with the hydrolysis of hemoglobin by the enzyme. However the removal of hemoglobin was apparently decreased with the increase of temperature over $60^{\circ}C$. 5. The removal of hemoglobin was relatively high at pH 7.0~8.0 and increased continuously with the increase of pH in detergency 6. In detergency, the removal mechanism of hemoglobin by subtilisin Carlsberg could be explained as follows: Fisrt of all, the enzyme hydrolyzed hemoglobin substrates partially by forming E-S complex at the surface of hemoglobin on the cotton fiber, and decomposed cooperative binding of hemoglobin. Subsequently, the fragments of hemoglobin were easily removed by washing. According as the enzyme penetrated to inner part of hemoglobin gradually, the hemoglobin on the cotton fiber was effectively removed by the repetition of these process. The removal of hemoglobin was more effectively increased by adding both the enzyme and AOS in the washing solution. Therefore, it was regarded that AOS molecules were adsorbed at the hydrophobic surface of denatured hemoglobin, subsequently, decomposed more effectively cooperative binding of hemoglobin, and the fragments of hemoglobin were removed more efficiently by means of the interfacial reaction of AOS.

• Journal of the Korean Society of Clothing and Textiles
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• v.20 no.3
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• pp.550-559
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• 1996

The Effect of protease (subtilisin Carlsberg) on the removal of hemoglobin as protein soil was studied. The hydrolysis characteristics of subtilisin Carlsberg was examined by electrophoretic techniques. The fragmentation patterns of hemoglobin were analyzed by SDS-PAGE. The hydrolysis efficiency was evaluated by analysis of protein bands shown on gels before and after hydrolysis by using densitometer. 1. The hydrolysis of hemoglobin by subtilisin Carlsberg was increased markedly with the increase of the enzyme concentration. 2. The hydrolysis of hemoglobin by subtilisin Carlsberg was effectively increased in proportion to increasing of the hemoglobin concentration up to a certain point, but it began to decrease above the point. 3. The hydrolysis of hemoglobin by subtilisin Carlsberg followed the first order kinetics, yielding a rate constant of $4.05\time10^{-4}S^{-1}s$. 4. The hydrolysis of hemoglobin by subtilisin Carlsberg was highest at $50^{\circ}C$ and was decreased markedly at $80^{\circ}C$. 5. The hydrolysis of hemoglobin was comparatively low at pH 7.0~8.0, and highest at pH 11.0.