Novel laccases of Ganoderma sp. KU-Alk4, regulated by different glucose concentration in alkaline media

Teerapatsakul, Churapa; Abe, Naoki; Bucke, C.; Kongkathip, Ngampong; Jareonkitmongkol, Saeree; Chitradon, Lerluck

doi:10.1007/s11274-007-9401-z

Cited by 25 publications

(34 citation statements)

References 41 publications

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“…Addition of glucose to culture media has been shown to influence laccase synthesis [37]. The concentration of glucose used in these studies varied from 0.1 to 1% [38].…”

Section: Discussionmentioning

confidence: 99%

Isolation and Physicochemical Characterization of Laccase fromGanoderma lucidum-CDBT1 Isolated from Its Native Habitat in Nepal

Shrestha

Joshi

et al. 2016

BioMed Research International

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At present, few organisms are known to and capable of naturally producing laccases and white rot fungi are one such group. In the present study, three fungal species, namely, Ganoderma lucidum-CDBT1, Ganoderma japonicum, and Lentinula edodes, isolated from their native habitat in Nepal were screened for laccase production, and G. lucidum-CDBT1 was found to express highest levels of enzyme (day 10 culture media showed 0.92 IU/mg total protein or 92 IU/mL laccase activity with ABTS as substrate). Lignin extracted from rice straw was used in Olga medium for laccase production and isolation from G. lucidum-CDBT1. Presence of lignin (5 g/L) and copper sulfate (30 μM) in the media increased the extracellular laccase content by 111% and 114%, respectively. The laccase enzyme produced by G. lucidum-CDBT1 was fractionated by ammonium sulfate and purified by DEAE Sepharose anion exchange chromatography. The purified enzyme was found to have a molecular mass of 43 kDa and exhibits optimal activity at pH 5.0 and 30°C. The isolated laccase was thermally stable for up to 70°C for 1 h and exhibited broad pH stability. The kinetic constants, K m, V max, and K cat, determined using 2,2′-azinobis-(-3-ethylbenzothiazoline-6-sulfonic acid) as substrate were found to be 110 μM, 36 μmol/min/mg, and 246 min−1, respectively. The isolated thermostable laccase will be used in future experiments for delignification process.

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“…Addition of glucose to culture media has been shown to influence laccase synthesis [37]. The concentration of glucose used in these studies varied from 0.1 to 1% [38].…”

Section: Discussionmentioning

confidence: 99%

Isolation and Physicochemical Characterization of Laccase fromGanoderma lucidum-CDBT1 Isolated from Its Native Habitat in Nepal

Shrestha

Joshi

et al. 2016

BioMed Research International

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“…No other ligninolytic enzymes are produced at pH 8.0. The crude enzyme has several isozymes of laccase (Teerapatsakul et al 2007b). The crude enzyme was stored at -80°C.…”

Section: Fungal Laccasementioning

confidence: 99%

Dye decolorisation by laccase entrapped in copper alginate

Teerapatsakul

Bucke

Parra‐Saldívar

et al. 2007

World J Microbiol Biotechnol

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A novel immobilisation system was developed for dye decolorisation using laccase produced by Ganoderma sp. KU-Alk4. The enzyme showed high efficiency in dye decolorisation when entrapped in Cu-Al and Cu-alginate beads. The former gave the highest activity but the enzyme activity survived longer in the latter. An experimental design of two 3 9 3 Latin Square experiments was applied to evaluate the effects of three different alginate compositions (low, intermediate and high mannuronate), concentration of alginate, (1.5, 3.0 and 4.5% w/v) and concentration of cross-linking agent, CuSO 4 (0.075, 0.15 and 0.225 M) on the decolorisation of indigo carmine dye and residual laccase activity in beads. The most significant factor for residual activity was the concentration of the cross-linking agent (P \ 0.05) followed by alginate composition (P \ 0.1). Increasing the alginate concentration resulted in only small increase in the dye decolorisation. However, higher laccase activity remained in 3.0% w/v alginate beads. Maximal dye decolorisation was achieved when 3.6% w/v low mannuronate alginate and 0.15 M CuSO 4 was used. Optimal conditions were confirmed in an extended experimental run. Results are presented from 9 successive batch runs over 12 days, reaching 96% removal of the dye (216 mg/l).

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“…The crude enzyme was composed of three dominant proteins which all exhibited 5 laccase activity. One protein was reported as a new laccase (Teerapatsakul et al, 2007a). 6 Immobilized enzyme was prepared from the crude enzyme described above in a copper 7 alginate bead.…”

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confidence: 99%

Repeated batch for dye degradation in an airlift bioreactor by laccase entrapped in copper alginate

Teerapatsakul

Parra‐Saldívar

Keshavarz

et al. 2017

International Biodeterioration & Biodegradation

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Abstract16 A repeated batch of synthetic dye decolorization was efficiently demonstrated in a 5 L airlift 17 bioreactor. A laccase from Ganoderma sp. KU-Alk4, degrading commercial aromatic dyes was 18 selected. The crude enzyme extract expressed laccase activity, and was immobilized under optimal 19 conditions in copper-alginate beads, 3 IU/bead. The immobilized enzyme showed high efficiency 20 in degrading various synthetic dyes under non-buffered conditions, in particular the indigoid dye 21 Indigo Carmine. The immobilized laccase also showed marked increase in stability toward 22 temperature and pH when compared with free enzyme preparation. Immobilization enhanced its 23 temperature stability to maintain initial activity up to 55 °C, ten degrees higher than the free 24 enzyme. The immobilized laccase was stable in the alkaline region up to pH 10.0. The dye 25 decolorization system in 5 L airlift bioreactor was demonstrated with 25 mg/L Indigo Carmine 26 dissolved in tap water and a total immobilized laccase activity of 6x10 4 IU. Airflow rate was the 27 most important factor affecting the number of batch runs and the time for 100% dye degradation. 28 An optimal airflow rate was of 4 L/min. Fourteen batch runs of complete dye degradation were 29 successfully completed with only a single enzyme supplementation, and this could be a feasible 30 system for operation in industry. Total dye degraded by this repeated process at 4 L/min airflow 31 rate was 1.8 g. Isatin sulfonic acid was a metabolic product of Indigo Carmine degradation 32 catalyzed by the immobilized laccase. This development of an effective repeatable bioprocess 33 using enzymes for the treatment of dye-contaminated effluent has potential for implementation on 34 an industrial scale.

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Novel laccases of Ganoderma sp. KU-Alk4, regulated by different glucose concentration in alkaline media

Cited by 25 publications

References 41 publications

Isolation and Physicochemical Characterization of Laccase fromGanoderma lucidum-CDBT1 Isolated from Its Native Habitat in Nepal

Isolation and Physicochemical Characterization of Laccase fromGanoderma lucidum-CDBT1 Isolated from Its Native Habitat in Nepal

Dye decolorisation by laccase entrapped in copper alginate

Repeated batch for dye degradation in an airlift bioreactor by laccase entrapped in copper alginate

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