• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.38 no.3 s.116
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• pp.13-22
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• 2006

The analogs of cyclic hydroxamic acids containing N-OH group have been proposed to play effective laccase-mediators in kraft pulp bleaching with laccase/mediator system. The existing mediators (NHA, 1-HBT, VA), the best laccase-mediators reported so far, and selected several analogs of cyclic hydroxamic acids were evaluated as a laccase-mediator for kraft pulp bleaching. It was found that NHA was the most effective mediator for the Trychophyton sp. LKY-7 laccase (TrL) in kraft pulp bleaching with TrL/mediator system, increasing about 10% ISO of brightness and decreasing about 2.8 of kappa number after alkaline-peroxide bleaching. Of the cyclic hydroxamic acidstested, the NHP.1(N-hydroxypyridone analog) was shown to enable TrL to effectively degrade lignin in kraft pulp bleaching, demonstrating approximately similar effect with that of NHA. However, the effect of substituent patterns of cyclic hydroxamic acid analogs in kraft pulp bleaching was not observed. The inhibitions of NHA and NHP.1 on TrL were not exhibited in TrL/mediator system. As a new mediator for TrL, NHP.1 was considered to be able to use in kraft pulp bleaching with TrL/mediator system.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.46 no.1
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• pp.1-10
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• 2014

Xylanase (X) derived from Aurreobasidium pullulans and laccase-mediator system (LM) using Trichophyton sp. LKY-7 laccase (TrL) and N-hydroxy-2-pyridone analogue (NHP) as a mediator were applied in hardwood kraft pulp (HwKP) bleaching. The individual and the synergistic effects of X and LM stage were investigated in the enzymatic bleaching of HwKP. Also, the effects of subsequent alkaline extraction (E) and alkaline/hydrogen peroxide treatment (P) were examined. In X or LM treatment alone, an appreciable bleaching effect of HwKP was not observed, whereas subsequent E or P stage enhanced the increase of brightness and the decrease of kappa number. Especially, P stage significantly enhanced the bleaching effect of pulp. Bleaching of HwKP with XLM sequentially gave significantly higher pulp brightness and lower kappa number than that obtained after the treatment of HwKP with X+LM simultaneously. When HwKP was sequentially treated with XLM followed by P stage, the brightness increased by about 11% ISO and the kappa number decreased by about 3.6 in comparison with the initial pulp. Xylanase and laccase were strongly inactivated by NHP both in the absence and the presence of pulp.

• Journal of Environmental Health Sciences
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• v.30 no.2
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• pp.79-83
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• 2004

The oxidative degradation of BPA with laccase from Trametes versiclor was conducted in a closed, temperature controlled system containing acetate buffer for pH control. The effects of medium pH, buffer concentration, temperature and mediator on degradation of BPA were investigated. The inactivation of the enzyme by temperature and reaction product was also studied. The optimal pH for BPA degradation showed about 5. Buffer concentration did not affect BPA degradation. On the other hand, the enzyme stability was higher at low concentration buffer(25 mM). Temperature rise increased the degradation rate of BPA up to 45$^{\circ}C$. The valuable mediator of laccase for BPA was ABTS. Elevated temperature and reaction product irreversibly inactivated the enzyme.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 2003.11a
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• pp.27-34
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• 2003

• Mycobiology
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• v.47 no.2
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• pp.217-229
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• 2019

Two manganese peroxidases (MnPs), MnP1 and MnP2, and a laccase, Lac1, were purified from Trametes polyzona KU-RNW027. Both MnPs showed high stability in organic solvents which triggered their activities. Metal ions activated both MnPs at certain concentrations. The two MnPs and Lac1, played important roles in dye degradation and pharmaceutical products deactivation in a redox mediator-free system. They completely degraded Remazol brilliant blue (25 mg/L) in 10-30 min and showed high degradation activities to Remazol navy blue and Remazol brilliant yellow, while Lac1 could remove 75% of Remazol red. These three purified enzymes effectively deactivated tetracycline, doxycycline, amoxicillin, and ciprofloxacin. Optimal reaction conditions were $50^{\circ}C$ and pH 4.5. The two MnPs were activated by organic solvents and metal ions, indicating the efficacy of using T. polyzona KU-RNW027 for bioremediation of aromatic compounds in environments polluted with organic solvents and metal ions with no need for redox mediator supplements.

• Journal of Microbiology and Biotechnology
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• v.23 no.6
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• pp.864-871
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• 2013

The recombinant strain P. pastoris GS115-lccC was used to produce laccase with high activity. Factors influencing laccase expression, such as pH, methanol concentration, copper concentration, peptone concentration, shaker rotate speed, and medium volume were investigated. Under the optimal conditions, laccase activity reached 12,344 U/L on day 15. The recombinant enzyme was purified by precipitating and dialyzing to electrophoretic homogeneity, and was estimated to have a molecular mass of about 58 kDa. When guaiacol was the substrate, the laccase showed the highest activity at pH 5.0 and was stable when the pH was 4.5~6.0. The optimal temperature for the laccase to oxidize guaiacol was $60^{\circ}C$, but it was not stable at high temperature. The enzyme could remain stable at $30^{\circ}C$ for 5 days. The recombinant laccase was used to degrade chlorpyrifos in several laccase/mediator systems. Among three synthetic mediators (ABTS, HBT, VA) and three natural mediators (vanillin, 2,6-DMP, and guaiacol), vanillin showed the most enhancement on degradation of chlorpyrifos. Both laccase and vanillin were responsible for the degradation of chlorpyrifos. A higher dosage of vanillin may promote a higher level of degradation of chlorpyrifos, and the 2-step addition of vanillin led to 98% chlorpyrifos degradation. The degradation of chlorpyrifos was faster in the L/V system ($k_{obs}$ = 0.151) than that in the buffer solution ($k_{obs}$ = 0.028).

• Journal of the Korean Wood Science and Technology
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• v.27 no.4
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• pp.1-14
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• 1999

As the biodegradation of wood constituents has been understood as a multi-basidiomycetes and enzymatic processes, this review will focus on the roles of low molecular compounds and radicals working in harmony with fungal enzymes. Wood rotting basidiomycete fungi penetrate wood, and lead to more easily metabolize carbohydrates of the wood complex. The white-rot fungi, having versatile enzymes, are able to attack directly the "lignin barrier". They also use a multi-enzyme system including so-called "feedback" type enzymes allowing for simultaneous degradation of lignin and carbohydrates. The multi-enzymes including laccase support the proposed route by explaining how the high molecular weight enzymes can function in the wood complex. These enzymes may function separately or cooperate each other. In addition, veratryl alcohol oxidase, cellobiose dehydrogenase, arylalcohol dehydrogenase, and particularly low molecular mediators and radicals have an important role in wood biodegradation. However, the possibility of other mechanism as well as other enzymes, as operating as feedback systems in the process of wood degradation, could not be excluded.