Laccase isoform diversity in basidiomycete Lentinus strigosus 1566: Potential for phenylpropanoid polymerization

Kolomytseva, M. P.; Myasoedova, N. M.; Chernykh, A.M.; Gaidina, Anastasya S.; Shebanova, Anna D.; Баскунов, Б. П.; Aschenbrenner, Jennifer; Rosengarten, Jamila Franca; Renfeld, Zh. V.; Gasanov, N. B.; Пинчук, И. П.; Claßen, Thomas; Pietruszka, Jörg; Golovleva, L. A.

doi:10.1016/j.ijbiomac.2019.07.056

Cited by 9 publications

(13 citation statements)

References 64 publications

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“…The product of condensation of three molecules of coniferyl alcohol ( R f 0.0) with successive elimination of the carbonyl group (CO) and ketene (CH 2 =C=O) or elimination of a fragment with m / z 71 ([ M +H] + 577 (70 %), 549 (25 %), 506 (100 %), 464 (15 %), 393 (25 %)) was found in a neutral extract of the reaction mixture containing the laccase of M. roridum VKM F‐3565. The trimeric polymers with a molecular ion mass [ M +H] + 433 and [ M H] + 447 were also found during coniferyl acid transformation catalyzed by the laccase of the basidiomycete L. strigosus 1566 [37] . The capability of the plant laccase from Rhus vernicifera to polymerize coniferyl alcohol and its analogues in a water/acetone solution have been also reported by Wan and co‐workers [35]…”

Section: Resultsmentioning

confidence: 58%

“…The polymeric products of ferulic acid transformation catalyzed by laccases were reported before. Thus, the laccase from basidiomycete Lentinus strigosus 1566 was capable of oxidizing ferulic acid resulting in the formation of the product of condensation of aromatic rings containing methoxy group and phenol hydroxyl, with [ M +H] + 233 [37] . As a result of the oxidation of ferulic acid by the laccase of the ascomycete M. verrucaria VKM F‐3851, a similar polymer product with [ M +H] + 233 was also found, however, it had a dissimilar MS‐spectrum of ionization, which indicates a different structure [38] .…”

Section: Resultsmentioning

confidence: 99%

“…0.01 mM syringaldazine, 0.1 mM ABTS, 2,6‐dimethoxyphenol, ferulic acid, and coniferyl alcohol were used as substrates. Absorbance of substrate or formed product was detected at corresponding wave‐length as described earlier [37] …”

Section: Methodsmentioning

confidence: 99%

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The Laccase of Myrothecium roridum VKM F‐3565: A New Look at Fungal Laccase Tolerance to Neutral and Alkaline Conditions**

et al. 2023

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Most of the currently known fungal laccases show their maximum activity under acidic environmental conditions. It is known that a decrease in the activity of a typical laccase at neutral or alkaline pH values is the result of an increase in the binding of the hydroxide anion to the T2/T3 copper center, which prevents the transfer of an electron from the T1 Cu to the trinuclear copper center. However, evolutionary pressure has resolved the existing limitations in the catalytic mechanism of laccase, allowing such enzymes to be functionally active under neutral/alkaline pH conditions, thereby giving fungi an advantage for their survival. Combined molecular and biochemical studies, homological modeling, calculation of the electrostatic potential on the Connolly surface at pH 5.0 and 7.0, and structural analysis of the novel alkaliphilic laccase of Myrothecium roridum VKM F‐3565 and alkaliphilic and acidophilic fungal laccases with a known structure allowed a new intramolecular channel near the one of the catalytic aspartate residues at T2‐copper atom to be found. The amino acid residues of alkaliphilic laccases forming this channel can presumably serve as proton donors for catalytic aspartates under neutral conditions, thus ensuring proper functioning. For the first time for ascomycetous laccases, the production of new trimeric products of phenylpropanoid condensation under neutral conditions has been shown, which could have a potential for use in pharmacology.

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Section: Resultsmentioning

confidence: 58%

Section: Resultsmentioning

confidence: 99%

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The Laccase of Myrothecium roridum VKM F‐3565: A New Look at Fungal Laccase Tolerance to Neutral and Alkaline Conditions**

et al. 2023

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“…CotA will oxidize ABTS resulting in a green-colored cationic radical (ABTS •+ ), which can be detected by measuring the absorption at wavelength 420 nm (ε = 36 000 M –1 cm –1 ). The relative activity was defined as the ratio between the specific activity of modified CotA and the specific activity of native CotA and expressed as a percentage. − The total protein concentration was determined using the BCA protein assay.…”

Section: Methodsmentioning

confidence: 99%

Charged Polypeptide Tail Boosts the Salt Resistance of Enzyme-Containing Complex Coacervate Micelles

et al. 2022

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Encapsulation of proteins can have advantages for their protection, stability, and delivery purposes. One of the options to encapsulate proteins is to incorporate them in complex coacervate core micelles (C3Ms). This can easily be achieved by mixing aqueous solutions of the protein and an oppositely charged neutral-hydrophilic diblock copolymer. However, protein-containing C3Ms often suffer from salt-inducible disintegration due to the low charge density of proteins. The aim of this study is to improve the salt stability of protein-containing C3Ms by increasing the net charge of the protein by tagging it with a charged polypeptide. As a model protein, we used CotA laccase and generated variants with 10, 20, 30, and 40 glutamic acids attached at the C-terminus of CotA using genetic engineering. Micelles were obtained by mixing the five CotA variants with poly( N -methyl-2-vinyl-pyridinium)- block -poly(ethylene oxide) (PM2VP 128 - b -PEO 477 ) at pH 10.8. Hydrodynamic radii of the micelles of approximately 31, 27, and 23 nm for native CotA, CotA-E20, and CotA-E40, respectively, were determined using dynamic light scattering (DLS) and fluorescence correlation spectroscopy (FCS). The encapsulation efficiency was not affected using enzymes with a polyglutamic acid tail but resulted in more micelles with a smaller number of enzyme molecules per micelle. Furthermore, it was shown that the addition of a polyglutamic acid tail to CotA indeed resulted in improved salt stability of enzyme-containing C3Ms. Interestingly, the polyglutamic acid CotA variants showed an enhanced enzyme activity. This study demonstrates that increasing the net charge of enzymes through genetic engineering is a promising strategy to improve the practical applicability of C3Ms as enzyme delivery systems.

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“…Mild conditions are conditions that have three conditions, which are: (i) low temperatures, (ii) under relative zero pressure, and (iii) without the usage of toxic solvents. However, we see the feasibility of a one-stage reaction to earn the needed compounds using laccases as biocatalysts to be particularly relevant (Myasoedova et al, 2008;Kolomytseva et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Testing for the ability to modify antibiotics of Panus tigrinus 8/18 Lentinus strigosus 1566 laccase

et al. 2024

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In advanced biotechnology, the utilization of enzymes to achieve new or modified compounds with antibacterial, fungicidal, and anti-cancer specifications is crucial. Mushroom lactases are a hopeful biocatalyst for the synthesis and modification of different compounds. They are an accessible and inexpensive enzyme for the preparation of reaction objects and have recently received attention. Laccase purification was performed from basidiomycete Lentinus strigosus (LS) in several stages: Stage 1. On ion-exchange chromatography on TEAE Servacell 23 (400 ml), two distinctly separated laccase activity peaks were observed, eluted from the carrier at 0.21 and 0.27 M NaCl. In order to reduce the loss of enzymes, all fractions with laccase activity were collected, concentrated, and desalted using an ultrafiltration cell (Amicon, United States) with a UM-10 membrane. Stage 2. The resulting preparation with laccase activity was applied to a Q-Sepharose column (60 ml). Two well-separated peaks with laccase activity were obtained during the elution: laccase I (0.12 M NaCl) and laccase II (0.2 M NaCl). Stage 3. In the course of further purification of both enzymes, carried out on anion-exchange carrier Resource Q (6 ml), a broken gradient was used: 0 - 10%, 10 - 20%, and 20 - 100% with 1M NaCl. Stage 4. Both laccase I and laccase II, obtained after Resource Q, were desalted, concentrated to 1 ml each, and applied to a Superdex 75 gel filtration column. As a result, two laccases were obtained in a homogeneous form.

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Laccase isoform diversity in basidiomycete Lentinus strigosus 1566: Potential for phenylpropanoid polymerization

Cited by 9 publications

References 64 publications

The Laccase of Myrothecium roridum VKM F‐3565: A New Look at Fungal Laccase Tolerance to Neutral and Alkaline Conditions**

The Laccase of Myrothecium roridum VKM F‐3565: A New Look at Fungal Laccase Tolerance to Neutral and Alkaline Conditions**

Charged Polypeptide Tail Boosts the Salt Resistance of Enzyme-Containing Complex Coacervate Micelles

Testing for the ability to modify antibiotics of Panus tigrinus 8/18 Lentinus strigosus 1566 laccase

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