Activity of Free and Immobilized Extracellular<i>Cerrena unicolor</i>Laccase in Water Miscible Organic Solvents

Luterek, Jolanta; Gianfreda, Liliana; Wojtas-Wasilewska, M.; Cho, N.S.; Rogalski, Jerzy; Jaszek, Magdalena; Malarczyk, Elżbieta; Staszczak, Magdalena; Fink-Boots, M.; Leonowicz, Andrzej

doi:10.1515/hfsg.1998.52.6.589

Cited by 39 publications

(23 citation statements)

References 38 publications

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“…LccA was relatively stable in all solvents examined, retaining nearly 75% of its activity after 24 h in methanol or ethanol and over 50% of its activity after incubation in DMSO or DMF. Prior studies (7,40,44,55,56) coupled with our current findings reveal that a wide variety of laccases, including LccA, are stable and/or can support catalysis and conversion of phenolic substrates in water-organic mixed solvents. Since most of the substrates and mediators of laccases are insoluble or poorly soluble in water and the degree of polymerization of phenoxyl radicals is higher in aqueous media (44), solvent stability is an important feature to consider in optimizing this group of enzymes.…”

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confidence: 68%

LccA, an Archaeal Laccase Secreted as a Highly Stable Glycoprotein into the Extracellular Medium by Haloferax volcanii

Uthandi

Boutaiba

Humbard

et al. 2010

Appl Environ Microbiol

116

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Laccases couple the oxidation of phenolic compounds to the reduction of molecular oxygen and thus span a wide variety of applications. While laccases of eukaryotes and bacteria are well characterized, these enzymes have not been described in archaea. Here, we report the purification and characterization of a laccase (LccA) from the halophilic archaeon Haloferax volcanii. LccA was secreted at high levels into the culture supernatant of a recombinant H. volcanii strain, with peak activity (170 ؎ 10 mU ⅐ ml ؊1 ) at stationary phase (72 to 80 h). LccA was purified 13-fold to an overall yield of 72% and a specific activity of 29.4 U ⅐ mg ؊1 with an absorbance spectrum typical of blue multicopper oxidases. The mature LccA was processed to expose an N-terminal Ala after the removal of 31 amino acid residues and was glycosylated to 6.9% carbohydrate content. Purified LccA oxidized a variety of organic substrates, including bilirubin, syringaldazine (SGZ), 2,2,-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and dimethoxyphenol (DMP), with DMP oxidation requiring the addition of CuSO 4 . Optimal oxidation of ABTS and SGZ was at 45°C and pH 6 and pH 8.4, respectively. The apparent K m values for SGZ, bilirubin, and ABTS were 35, 236, and 670 M, with corresponding k cat values of 22, 29, and 10 s ؊1 , respectively. The purified LccA was tolerant of high salt, mixed organosolvents, and high temperatures, with a half-life of inactivation at 50°C of 31.5 h.Multicopper oxidases (MCOs) are a family of enzymes that include laccases (p-diphenol: dioxygen oxidoreductases; EC 1.10.3.2), ascorbate oxidases (EC 1.10.3.3), ferroxidases (EC 1.16.3.1), bilirubin oxidases (EC 1.3.3.5), and other enzyme subfamilies (27,65). MCOs couple the oxidation of organic and/or inorganic substrates to the four-electron reduction of molecular oxygen to water. These enzymes often have four Cu atoms classified into type 1 (T1), type 2 (T2), and type 3 (T3) centers, in which a mononuclear T1 center on the surface of the enzyme provides long-range intramolecular one-electron transfer from electron-donating substrates to an internal trinuclear T2-T3 center formed by a T2 Cu coordinated with a T3 Cu pair. The T2-T3 cluster subsequently reduces dioxygen to water.Enzymes of the laccase subfamily oxidize a broad range of compounds, including phenols, polyphenols, aromatic amines, and nonphenolic substrates, by one-electron transfer to molecular oxygen and thus have a wide variety of applications from biofuels to human health. The best-known application is the use of a laccase from the lacquer tree Rhus vernicifera in paint and adhesives for more than 6,000 years in East Asia (29). Laccases have also been used in the delignification of pulp, bleaching of textiles and carcinogenic dyes, detoxification of water and soils, removal of phenolics from wines, improving adhesive properties of lignocellulosic products, determination of bilirubin levels in serum, and transformation of antibiotics and steroids (60). In addition, laccases have demonstrated pote...

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confidence: 68%

LccA, an Archaeal Laccase Secreted as a Highly Stable Glycoprotein into the Extracellular Medium by Haloferax volcanii

Uthandi

Boutaiba

Humbard

et al. 2010

Appl Environ Microbiol

116

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“…It was determined by the oxidation rate of ABTS molecules over time. According to Luterek et al (1998) the highest activity of the enzyme is achieved at the pH between 5.3 and 5.8. Therefore, pH = 5.7 sodium acetic acid buffer was prepared.…”

Section: Activity Measurementsmentioning

confidence: 99%

Partitioning of cerrena unicolor laccase activity in an aqueous two-phase system

Blatkiewicz

Górak

Ledakowicz

2016

Chemical and Process Engineering

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Culture supernatant containing laccase produced by Cerrena unicolor strain was used to examine laccase partitioning between phases in an aqueous two-phase system. The investigated system consisted of polyethylene glycol 3000 and sodium phosphate buffer adjusted to pH = 7. Influence of several parameters on partitioning was measured, including phase forming components' concentrations, tie line lengths, phase volume ratio, supernatant dilution, process temperature and halogen salt supplementation. Partitioning coefficients up to 78 in the bottom phase were achieved with yields of over 90%. Tie line length and phase volume ratio had significant effect on enzyme partitioning.

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“…However, the laccase may be denatured or it may be inhibited under these conditions [329,330]. In this regard laccases can be applied in nonaqueous solution or multiphasic systems.…”

Section: Potential New Laccase-based Biocatalystsmentioning

confidence: 99%

Laccases and Their Applications: A Patent Review

Kunamneni

Plou²,

Ballesteros³

et al. 2008

BIOT

276

172

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Abstract:Laccases are an interesting group of multi copper enzymes, which have received much attention of researchers in last decades due to their ability to oxidize both phenolic and non-phenolic lignin related compounds as well as highly recalcitrant environmental pollutants. This makes these biocatalysts very useful for their application in several biotechnological processes. Such applications include the detoxification of industrial effluents, mostly from the paper and pulp, textile and petrochemical industries, polymer synthesis, bioremediation of contaminated soils, wine and beverage stabilization. Laccases are also used as catalysts for the manufacture of anti-cancer drugs and even as ingredients in cosmetics. Recently, the utility of laccases has also been applied to nanobiotechnology. This paper reviews recent and important patents related to the properties, heterologous production, molecular cloning, and applications of laccases within different industrial fields as well as their potential extension to the nanobiotechnology area.

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Activity of Free and Immobilized ExtracellularCerrena unicolorLaccase in Water Miscible Organic Solvents

Cited by 39 publications

References 38 publications

LccA, an Archaeal Laccase Secreted as a Highly Stable Glycoprotein into the Extracellular Medium by Haloferax volcanii

LccA, an Archaeal Laccase Secreted as a Highly Stable Glycoprotein into the Extracellular Medium by Haloferax volcanii

Partitioning of cerrena unicolor laccase activity in an aqueous two-phase system

Laccases and Their Applications: A Patent Review

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