• Fashion & Textile Research Journal
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• v.2 no.4
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• pp.339-345
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• 2000

The effects of protease and/or lipase on the removal of protein soil and oily soil were investigated in this study. Cotton, rayon, nylon, and PET fabrics were soiled by padding of fresh bovine blood and spotting of mixed artificial sebum evenly. The soiled fabrics were aged at $130^{\circ}C$ for 30 minutes. The fabrics were washed by using Terg-O-Tometer at various conditions. Protease and/or lipase were added in the alcohol ethoxylate (AE) detergent solution. The removal efficiency was evaluated by analysis of protein and/or oil on the fabrics before and after washing, respectively. The detergency of protein and/or oil on the fabrics was discussed with enzyme concentration, washing time, washing temperature, pH of washing solution and fiber characteristics. The hydrolysis of protease improved effectively the removal of oil as well as protein by increasing removal of protein-oil mixed soil at the same time. The effect of lipase added detergent solution was slightly shown on the removal of oil and/or protein. The removal of mixed soils from cotton fabrics was very low because of large amount of residual soils caused by the physical characteristics of cotton fiber.

• Journal of Microbiology and Biotechnology
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• v.6 no.1
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• pp.36-42
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• 1996

The production of sorbitol by permeabilized cells of Zymomonas mobilis immobilized in $\kappa$-carrageenan was investigated. Cetyltrimethylammoniumbromide (CTAB) permeabilized cells were treated with glutaraldehyde prior to immobilization for cross-linking of enzymes, glucose-fructose oxidoreductase (GFOR) in cells. Rigidity of the immobilized beads was increased two-fold with 90$\%$ conversion efficiency by the additions of 40$\%$ (w/v) polyols (glycerol 25 g + propylene glycol 15 g) to 60$\%$ (w/v) distilled water containing 2.5$\%$ (w/v) $\kappa$-carrageenan as a final concentration, prior to immobilization. $\kappa$-Carrageenan beads entrapping permeabilized cells were dried to improve bead rigidity and storage stability. During s6mi-batch process for 72 h with dry beads, there was an improvement of the loss of enzyme activity (less than 10$\%$). In batch process, the kinetic results of $K_m.fructose$ value for the free cells, wet beads and dry $\kappa$-carrageenan beads were 71.7, 72.4 and 116.7 g/l, respectively. Higher productivity was obtained with two-stage continuous packed bed reactors with both wet and dry $\kappa$-carrageenan beads at 25.00 and 21.15 g/l/h, respectively, when measured at second stage.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.48 no.3
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• pp.37-43
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• 2016

Various mechanical and chemical pretreatment methods including alkali treatment, pre-beating, enzyme treatment and oxidation treatment have been used to reduce the production energy of the microfibrillated cellulose (MFC). Among them, alkali swelling can be helpful to reduce the energy consumption because the internal bonding between fibrils could be weakened. In this study, dimethyl sulfoxide (DMSO) was used as a cosolvent to improve alkali pretreatment efficiency and the effects of NaOH concentration during NaOH-DMSO swelling on changes in fiber characteristics of softwood bleached kraft pulp (SwBKP) were elucidated. For alkali treatment in H2O-DMSO solvents, fiber length were decreased with increasing NaOH concentration while fiber width, curl and WRV were increased. WRV began to increase at 8% NaOH solution. In addition, above 8% concentration of NaOH, crystalline structure of pulp fibers converted from cellulose II to cellulose III by DMSO cosolvent. Comparing the previous results with this study, it was shown that DMSO cosolvent could promote swelling of pulp fibers and thus reduce NaOH concentration for the maximum swelling of fibers.

• Microbiology and Biotechnology Letters
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• v.3 no.1
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• pp.17-22
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• 1975

Studies on the elimination of tannin from the acorns containing tannin up to 9%, for the utilization of the acorns in Korea, carried out as follows: 1. The strain of Asp. niger sp. which yield the reasonable enzymatic activity of tannase was isolated from the rotten acorns. 2. The method of hydrolyzing tannin in the water by suspending, and agitatiag the acorn powder: followed by decantation, showed the best result aomng the conventional methods in the efficiency of removal of tannin and in the economy of the process by reducing the tannin content to 0.18％ in 24 hours. 3. It was notable that the acorn'powder from which the tannin was eliminated contains various essential amino acids in relatively ample a mount.

• BMB Reports
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• v.30 no.5
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• pp.308-314
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• 1997

We investigated biotinylation of nitrocellulose membrane for immuno-filtration capture assay. In order to enhance the efficiency of biotinylation, nitrocellulose membranes were pretreated with several chemicals for the purpose of suitable protein absorption through surface modification. As a signal generating enzyme, urease was used and the concentration of avidin was optimized for the efficient binding kinetics between urease-biotin in liquid phase and biotinylated membrane in solid phase. For effective biotinylation, bovine serum albumin-biotin complexes could be immobilized at a concentration of $370\;{\mu}g$/stick ($4.4\;cm^2$). Among tested chemicals, polylysine (0.25%) showed a significant effect in biotinylation. Polylysine is thought to enhance surface area by extending unbound residues into solution. Time of treatment over 30 min and higher molecular weight of polylysines (58,100 dalton) showed positive effect on the enhancement of biotinylation. The result from this study may be useful for developing a new biosensor and other biofunctional membranes for examining molecular recognition.

• Journal of the Korean Society of Clothing and Textiles
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• v.30 no.11 s.158
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• pp.1572-1582
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• 2006

In this study, in order to compare a Tencel/cotton and a Tencel/Cotton/PET as Tencel blended fabrics with a Tencel fabric, the fabric samples were treated with chitosan after NaOH pretreatment and enzyme treatment thereof, And then its adherent efficiency was enhanced by using a crosslinking agent. After that, it was treated with a softener. In chitosan treatment, the functions of moisture regain, tensile strength, air permeability and crease resistance were more improved in the Tencel blended fabrics than in the Tencel fabric. Thus, it may be thought that the physical properties of the Tencel blended fabrics were more effectively modified than those of the Tencel fabric. And the friction charged voltage was very much reduced in all samples, so that chitosan treatment was effective for prevention of electrostatic charge. Further, chitosan finishing treatment improved remarkably the antibacterial activity in all samples regardless of the type of strains.

• Journal of Microbiology and Biotechnology
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• v.26 no.5
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• pp.829-836
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• 2016

Penicillin G acylase (PGA) was immobilized on magnetic Fe₃O₄@chitosan nanoparticles through the Schiff base reaction. The immobilization conditions were optimized as follows: enzyme/support 8.8 mg/g, pH 6.0, time 40 min, and temperature 25 ℃. Under these conditions, a high immobilization efficiency of 75% and a protein loading of 6.2 mg/g-support were obtained. Broader working pH and higher thermostability were achieved by the immobilization. In addition, the immobilized PGA retained 75% initial activity after ten cycles. Kinetic parameters V_max and K_m of the free and immobilized PGAs were determined as 0.113 mmol/min/mg-protein and 0.059 mmol/min/mg-protein, and 0.68 mM and 1.19 mM, respectively. Synthesis of amoxicillin with the immobilized PGA was carried out in 40% ethylene glycol at 25 ℃ and a conversion of 72% was obtained. These results showed that the immobilization of PGA onto magnetic chitosan nanoparticles is an efficient and simple way for preparation of stable PGA.

• Journal of Microbiology and Biotechnology
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• v.24 no.6
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• pp.788-794
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• 2014

An extracellular ${\beta}$-glucosidase from Aspergillus niger Au0847 was purified to homogeneity by precipitation with ammonium sulfate, anion exchange, and gel filtration. The purified protein was composed of two subunits with molecular masses of 110 and 120 kDa. Au0847 ${\beta}$-glucosidase exhibited relatively high thermostability and pH stability, and its highest activity was obtained at $65^{\circ}C$ and pH 4.6, respectively. As a potential metalloprotein, its enzymatic activity was potently stimulated by manganese ion and DTT. The ${\beta}$-glucosidase displayed avid affinity and high catalytic efficiency for geniposide. Au0847 ${\beta}$-glucosidase has potential value as an industrial enzyme for the hydrolysis of geniposide to genipin.

• Microbiology and Biotechnology Letters
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• v.24 no.6
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• pp.743-748
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• 1996

For the biological treatment of phenolic resin wastewater containing phenol and formaldehyde, a phenol-degrading yeast was isolated from the papermill sludge, and then identified as Candida tropicalis PW-51 according to morphological, physiological and biochemical properties. The strain was able to degrade high phenol concentrations up to 2,000mg/l within 58 hours in batch cultures. Phenol-degrading efficiency by the strain was maximum at the culture conditions of a final concentration of 9 $\times$ 10$^{6}$ cells/ml, 30$\circ$C and pH 7.0. The mean degradation rate of phenol was highest at 45.5mg/l/h in 1,000mg/l phenol from 500mg/l to 2,000mg/l phenol. Because the enzyme activity of catechol 1,2-dioxygenase increased in the course of degradation of phenol, it seems that this strain degrades phenol via the ortho-cleavage of benzene ring. The isolate C. tropicalis PW-51 could be effectively used for the biological treatment of phenolic resin wastewater.

• Journal of Microbiology and Biotechnology
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• v.13 no.5
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• pp.767-772
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• 2003

Three plasmids derived from the ${\beta}-agarase$ gene (PjaA) of Pseudomonas sp. W7 were expressed in Escherichia coli AD494(DE3) pLysS with lactose as an inducer. These products corresponded to the complete (PjaA) and the two C-terminal truncated (PjaAI and PjaAII) forms of ${\beta}-agarase$. The PjaAI and the PjaAII were originated from exonuclease L treatment from PjaA by deleting 127 and 182 amino acid residues-encoded nucleic acids at 3' region, respectively. The molecular weights of the purified proteins were 71 kDa, 58 kDa, and 50 kDa on SDS-PAGE, respectively. The $K_m$ value of PjaAI was lower than that of the PjaA, and the catalytic efficiency ($k_{cat}/K_m$) of PjaAI was increased to 5 times. The enzyme of PjaAI retained more than 90% activity at $50^{\circ}C$. In contrast to the PjaAI, the remaining activity of the PjaA was only 20% at the same temperature.