Two laccase isoforms of the basidiomycete <i>Cerrena unicolor</i> VKMF‐3196. Induction, isolation and properties

Lisova, Zoya A.; Lisov, A. V.; Leontievsky, A. A.

doi:10.1002/jobm.200900382

Cited by 40 publications

(31 citation statements)

References 45 publications

(28 reference statements)

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“…Among them, copper and aromatic compounds are considered as the most potent inducers of enzyme synthesis (Revankar and Lele 2006; Elisashvili and Kachlishvili 2009; Lisova et al 2010; Janusz et al 2013). In this study, supplementing the culture medium with 1 mM CuSO 4 or 1 mM xylidine significantly accelerated laccase secretion and increased enzyme yield (Figure 2).…”

Section: Discussionmentioning

confidence: 99%

“…There are few reports on the production of LME by the Cerrena unicolor strains (Janusz et al 2007; Lisova et al 2010; Songulashvili et al 2012; Hibi et al 2012; Rola et al 2013). However, the knowledge related to the physiological regulation of C. unicolor LME synthesis is limited to develop economical ways of industrial scale enzyme production.…”

Section: Introductionmentioning

confidence: 99%

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Modulation of Cerrena unicolor laccase and manganese peroxidase production

2014

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Among seven carbon sources tested, glycerol and glucose favored the Cerrena unicolor laccase production (18.8-20.3 U/mL); in addition, glycerol ensured the highest manganese peroxidase (MnP) activity (2 U/mL). Substitution of glycerol with the ethanol production residue (EPR) gave the highest laccase (90.1 U/mL) activity, while the walnut pericarp provided the highest MnP activity (7.4 U/mL). Supplementation of medium with 1 mM copper and 1 mM xylidine at appropriate time caused significant additive effect on laccase expression (333.2 U/mL) in shake-flask experiments. Overproduction of laccase activity (507 U/mL) and secretion of MnP activity was obtained when C. unicolor was cultivated in stirred-tank fermenter. C. unicolor showed several distinctive and attractive technological features: it is capable to synthesize high levels of oxidases under high carbon and high nitrogen conditions and it secretes high laccase activity during trophophase.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Modulation of Cerrena unicolor laccase and manganese peroxidase production

2014

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“…The molecular weight of the laccase from S. commune was reported to be 62 KDa by SDS-PAGE [De Vries et al, 1986], suggesting the carbohydrate content to be around 13.7%. The variations in the experimental findings could be due to the presence of many laccase isoforms with different characteristics [Dong et al, 2005;Giardina et al, 2007;Lisova et al, 2010]. Slight variations in the expressed peptide sequences are attributed to differences in patterns of glycosylation in P. pastoris contributing to the differences observed.…”

Section: Discussionmentioning

confidence: 99%

Enhanced delignification of lignocellulosic substrates by <i>Pichia</i> GS115 expressed recombinant laccase

Kumar

Kolte

Dhali

et al. 2018

J. Gen. Appl. Microbiol.

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Utilization of energy-rich crop residues by ruminants is restricted by the presence of lignin, which is recalcitrant to digestion. Application of lignin degrading enzymes on the lignocellulosic biomass exposes the cellulose for easy digestion by ruminants. Laccases have been found to be considerably effective in improving the digestibility by way of delignification. However, laccase yields from natural hosts are not sufficient for industrial scale applications, which restricts their use. A viable option would be to express the laccase gene in compatible hosts to achieve higher production yields. A codon-optimized synthetic variant of Schizophyllum commune laccase gene was cloned into a pPIC9K vector and expressed in P. pastoris GS115 (his4) under the control of an alcohol oxidase promoter. Colonies were screened for G418 resistance and the methanol utilization phenotype was established. The transformant yielded a laccase activity of 344 U . mL -1 after 5 days of growth at 30 0 C (0.019 g . mL -1 wet cell weight). The laccase protein produced by the recombinant Pichia clone was detected as two bands with apparent molecular weights of 55 kDa and 70 kDa on SDS-PAGE. Activity staining on native PAGE confirmed the presence of bioactive laccase. Treatment of five common crop residues with recombinant laccase recorded a lignin loss ranging between 1.64% in sorghum stover, to 4.83% in finger millet, with an enhancement in digestibility ranging between 8.71% in maize straw to 24.61% in finger millet straw.Treatment with recombinant laccase was effective in enhancing the digestibility of lignocellulosic biomass for ruminant feeding through delignification. To date, a number of hosts have been adventured to produce laccase in large quantities, but, to our knowledge, there are no reports of the expression of laccase protein from Schizophyllum commune in Pichia pastoris, and also on the treatment of crop residues using recombinant laccase for ruminant feeding.

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“…The laccase-inducing ability of guaiacol is observed in many basidomycetes, but there is not sufficient evidence of the molecular mechanism of laccase regulation by an inducer. [16,37,38] In the static culture, 8 times more laccase was obtained using 0.906 mM guaiacol added at 96 hr of fermentation compared to the enzyme obtained without using any inducer (without inducer, laccase activity 26 U=L). For the same concentration and time of addition of guaiacol, 40 times higher laccase production was observed in the shake culture than that obtained without any inducer (without inducer laccase activity $4 U=L) (cf.…”

Section: Screening Of Medium Constituents and Their Optimization For mentioning

confidence: 99%

Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced byDaedalea flavida

Singha¹,

Panda²

2014

Preparative Biochemistry and Biotechnology

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Studies on laccase production by Daedalea flavida were carried out in static and low-speed shake cultures. The enzyme production was reduced drastically at a high speed of shaking. Optimal production conditions are necessary to assess the quality of laccase suitable for a specific application. Thus, the production of laccase was optimized by the application of response surface methodology. Laccase production was 8-fold and 7.5-fold more in static and low-speed shake conditions, respectively, in an optimal medium composition than in an unoptimized medium. Laccase obtained using the optimal culture medium of D. flavida was tested for its stability at different temperatures and pH conditions. The partially purified enzyme was most stable at 30°C and pH 5. The half-life of laccase is 87 min at 60°C and at pH 6. The kinetic and thermodynamic parameters were evaluated for the inactivation of the partially purified laccase. The entropy change of inactivation of the enzyme is least at pH 4.

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Two laccase isoforms of the basidiomycete Cerrena unicolor VKMF‐3196. Induction, isolation and properties

Cited by 40 publications

References 45 publications

Modulation of Cerrena unicolor laccase and manganese peroxidase production

Modulation of Cerrena unicolor laccase and manganese peroxidase production

Enhanced delignification of lignocellulosic substrates by <i>Pichia</i> GS115 expressed recombinant laccase

Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced byDaedalea flavida

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