Production, Gene Cloning, and Overexpression of a Laccase in the Marine-Derived Yeast Aureobasidium melanogenum Strain 11-1 and Characterization of the Recombinant Laccase

Aung, Thu; Jiang, Hong; Chen, Chengcheng; Liu, Guanglei; Huang, Zhong; Chi, Zhen‐Ming; Chi, Zhe

doi:10.1007/s10126-018-9860-2

Cited by 20 publications

(10 citation statements)

References 37 publications

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“…Moreover, G3 laccase is the first enzyme of its kind for which activity was also observed at 0 and 4 • C. Most of the known multicopper oxidases are thermophilic enzymes characterized by high optimal operating temperatures, and the fungal laccases from the literature usually have T opt of 50-60 • C [29,35,45,[71][72][73][74]. Homologues with lower T opt were also described, e.g., laccases from A. pullulans [51,52], Monilinia fructicola [39], Aureobasidium melanogenum [75], V. volvacea V14 [31] and Cerrena sp. HYB07 [72] operate at high activity at 30-45 • C, similarly to the K. bupleuri laccase reported in this study.…”

Section: Properties Of the Preliminary Purified K Bupleuri Laccase G3mentioning

confidence: 99%

“…Laccase produced by K. bupleuri was used in the decolorization of methylene blue, alkaline fuchsin, crystal violet and Coomassie Brilliant Blue R-250 (Table 3). The optimum pH in reaction with ABTS observed for fungal laccases is most often in the range of 3.0-4.0 [16,28,31,35,45,72,75]. A slightly higher value, pH 5.0, was noted for A. pullulans laccases [51] and for Thielavia sp.…”

Section: Application Of Laccase In Synthetic Dye Decolorization Processmentioning

confidence: 99%

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Screening of Novel Laccase Producers—Isolation and Characterization of Cold-Adapted Laccase from Kabatiella bupleuri G3 Capable of Synthetic Dye Decolorization

2021

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Psychrophilic laccases catalyzing the bond formation in mild, environmentally friendly conditions are one of the biocatalysts at the focus of green chemistry. Screening of 41 cold-adapted strains of yeast and yeast-like fungi revealed a new laccase-producing strain, which was identified as Kabatiella bupleuri G3 IBMiP according to the morphological characteristics and analysis of sequences of the D1/D2 regions of 26S rDNA domain and the ITS1–5,8S–ITS2 region. The extracellular activity of laccase in reaction with 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) at the optimal pH 3.5 was 215 U/L after 15 days of growth in a medium with waste material and 126 U/L after 25 days of cultivation in a defined medium. Copper (II) ions (0.4 mM), Tween 80 (1.0 mM) and ascorbic acid (5.0 mM) increased the production of laccase. The optimum temperature for enzyme operation is in the range of 30–40 °C and retains over 60% of the maximum activity at 10 °C. New laccase shows high thermolability—half-life at 40 °C was only 60 min. Enzyme degradation of synthetic dyes was the highest for crystal violet, i.e., 48.6% after 1-h reaction with ABTS as a mediator. Outcomes of this study present the K. bupleuri laccase as a potential psychrozyme for environmental and industrial applications.

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Section: Properties Of the Preliminary Purified K Bupleuri Laccase G3mentioning

confidence: 99%

Section: Application Of Laccase In Synthetic Dye Decolorization Processmentioning

confidence: 99%

Screening of Novel Laccase Producers—Isolation and Characterization of Cold-Adapted Laccase from Kabatiella bupleuri G3 Capable of Synthetic Dye Decolorization

2021

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“…(ADK66266.1), and Aureobasidium pullulans (AUW14931.1). The results reflect that L01 has typical conserved motifs appearing in laccases, such as “HPXHXHGHXF”, “WYHPH”, “HWHGI”, “HPXHXHGHXF”, and “HCH” ( Figure 2 ), which are verified copper-binding domains [ 12 , 13 , 14 , 15 , 16 ]. Thus, according to bioinformatics analysis, L01 is a typical laccase.…”

Section: Resultsmentioning

confidence: 66%

“…Most bacterial laccases exhibit their highest activity below 40 °C. Most laccases have an activity of less than half of the highest level below 30 °C [ 12 , 22 , 23 , 24 , 25 , 26 , 27 ]. In contrast, L01 exhibits higher activity at 10 °C and 20 °C and relatively better thermostability compared to that of other laccases, which indicates that L01 is a typical cold-adapted laccase.…”

Section: Resultsmentioning

confidence: 99%

Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Jiang

Deng

Wang³

et al. 2023

Molecules

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Laccases have been widely used for fruit juice clarification, food modification, and paper pulp delignification. In addition, laccases exhibit remarkable performance in the degradation of toxic substances, including pesticides, organic synthetic dyes, antibiotics, and organic pollutants. Thus, the screening and development of robust laccases has attracted significant attention. In this study, Vibrio sp. LA is a strain capable of producing cold-adapted laccases. The laccase coding gene L01 was cloned from this strain and expressed in Yarrowia lipolytica, a host with good secretion ability. The secreted L01 (approximate MW of 56,000 Da) had the activity and specific activity of 18.6 U/mL and 98.6 U/mg toward ABTS, respectively. The highest activity occurred at 35 °C. At 20 °C, L01 activity was over 70% of the maximum activity in pH conditions ranging from 4.5–10.0. Several synthetic dyes were efficiently degraded by L01. Owing to its robustness, salt tolerance, and pH stability, L01 is a promising catalytic tool for potential industrial applications.

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“…ABTS is the most popular substrate used in the study of laccase activity. The optimum pH values for such reactions are most often in the range of 3.0-4.0 [35,40], however, there are also laccases characterized by slightly higher optimal pH reaching the values of 5.0, e.g., for the laccase from A. pullulans [41] and Thielavia sp. [42], and pH 6.0 for the laccase from Thermus thermophilus [43].…”

Section: Characterization Of Purified Kblcc1 Laccase 231 Influence Of Ph and Temperature On Purified Laccase Kblcc1 Activity And Stabilitmentioning

confidence: 99%

Novel Cold-Adapted Recombinant Laccase KbLcc1 from Kabatiella bupleuri G3 IBMiP as a Green Catalyst in Biotransformation

Wiśniewska

Twarda-Cłapa

Białkowska

2021

IJMS

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Cold-adapted enzymes are useful tools in the organic syntheses conducted in mixed aqueous-organic or non-aqueous solvents due to their molecular flexibility that stabilizes the proteins in low water activity environments. A novel psychrophilic laccase gene from Kabatiella bupleuri, G3 IBMiP, was spliced by Overlap‑Extension PCR (OE-PCR) and expressed in Pichia pastoris. Purified recombinant KbLcc1 laccase has an optimal temperature of 30 °C and pH of 3.5, 5.5, 6.0, and 7.0 in the reaction with 2,2′‑azino‑bis(3‑ethylbenzothiazoline‑6‑sulfonic acid) (ABTS), guaiacol, sinapic acid, and syringaldazine, respectively. Moreover, laccase KbLcc1 is highly thermolabile, as it loses 40% of activity after 30 min at 40 °C and is inactivated at 50 °C after the same period of incubation. The new enzyme remained active with 1 mM of Ni2+, Cu2+, Mn2+, and Zn2+ and with 2 mM of Co2+, Ca2+, and Mg2+, but Fe2+ greatly inhibited the laccase activity. Moreover, 1% ethanol had no impact on KbLcc1, although acetone and ethyl acetate decreased the laccase activity. The presence of hexane (40%, v/v) caused a 58% increase in activity. Laccase KbLcc1 could be applied in the decolorization of synthetic dyes and in the biotransformation of ferulic acid to vanillin. After 5 days of reaction at 20 °C, pH 3.5, with 1 mM ABTS as a mediator, the vanillin concentration was 21.9 mg/L and the molar yield of transformation reached 14.39%.

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Production, Gene Cloning, and Overexpression of a Laccase in the Marine-Derived Yeast Aureobasidium melanogenum Strain 11-1 and Characterization of the Recombinant Laccase

Cited by 20 publications

References 37 publications

Screening of Novel Laccase Producers—Isolation and Characterization of Cold-Adapted Laccase from Kabatiella bupleuri G3 Capable of Synthetic Dye Decolorization

Screening of Novel Laccase Producers—Isolation and Characterization of Cold-Adapted Laccase from Kabatiella bupleuri G3 Capable of Synthetic Dye Decolorization

Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Novel Cold-Adapted Recombinant Laccase KbLcc1 from Kabatiella bupleuri G3 IBMiP as a Green Catalyst in Biotransformation

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