Characterization of recombinant laccase from Trametes versicolor synthesized by Arxula adeninivorans and its application in the degradation of pharmaceuticals

The forest products industry has a very important role in the development toward a sustainable, biobased society. However, many fungi that deteriorate the main structural components of wood, such as cellulose, hemicellulose and lignin, are able to cause decay in standing trees, leading to significant losses in forest output due to impacts on biomass production. Trametes versicolor (L.: Fr) Pilát is a fungus able to attack the trees by saprotrophic and parasitic life strategies, causing white-rot of wood species, a serious problem for the industry that is focused on wood and its uses. The objectives of the work were the synthesis of organotin(IV) carboxylate of a natural product (ent-kaurenoic acid), characterization of the structures and anti-fungal evaluation against T. versicolor, as a contribution of new alternatives for the wood preservation. The synthesis of organotin(IV) complexes derived from the diterpene tetracyclic ent-kaur-16-en-19-oic acid (ent-kaurenoic acid, KA) gave three new complexes potentially active against T. versicolor. The complexes were characterized by FTIR and NMR spectroscopy. The biological activity was evaluated by a gel dilution method with superficialplate inoculation, using 60 and 120 μg/mL concentration, for the KA and the three organotin(IV) complexes. A considerably higher bioactivity was observed to the 120 μg/mL concentration, and for the complex with greater molecular weight.

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Cloning and Characterization of a cDNA Encoding a Novel Extracellular Peroxidase from Trametes versicolor

Applied and Environmental Microbiology ◽

10.1128/aem.65.3.1343-1347.1999 ◽

1999 ◽

Vol 65 (3) ◽

pp. 1343-1347 ◽

Cited By ~ 24

Author(s):

Patrick J. Collins ◽

Margaret M. O’Brien ◽

Alan D. W. Dobson

Keyword(s):

Trametes Versicolor ◽

Cdna Sequence ◽

White Rot ◽

Transcript Levels ◽

Extracellular Peroxidase ◽

Low Concentrations ◽

Lignin Peroxidases

ABSTRACT The white rot basidiomycete Trametes versicolorsecretes a large number of peroxidases which are believed to be involved in the degradation of polymeric lignin. These peroxidases have been classified previously as lignin peroxidases or manganese peroxidases (MnP). We have isolated a novel extracellular peroxidase-encoding cDNA sequence from T. versicolor CU1, the transcript levels of which are repressed by low concentrations of Mn2+ and induced by nitrogen and carbon but not induced in response to a range of stresses which have been reported to induce MnP expression.

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Comparative characterization of four laccases from Trametes versicolor concerning phenolic C–C coupling and oxidation of PAHs

Archives of Biochemistry and Biophysics ◽

10.1016/j.abb.2008.03.009 ◽

2008 ◽

Vol 474 (1) ◽

pp. 213-219 ◽

Cited By ~ 53

Author(s):

Katja Koschorreck ◽

Sven M. Richter ◽

André Swierczek ◽

Uwe Beifuss ◽

Rolf D. Schmid ◽

...

Keyword(s):

Trametes Versicolor ◽

Comparative Characterization

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Characterization of a lignin peroxidase gene from the white-rot fungus Trametes versicolor

Biochimie ◽

10.1016/0300-9084(92)90043-e ◽

1992 ◽

Vol 74 (2) ◽

pp. 177-182 ◽

Cited By ~ 26

Author(s):

L. Jönsson ◽

P.O. Nyman

Keyword(s):

Lignin Peroxidase ◽

Trametes Versicolor ◽

White Rot ◽

White Rot Fungus ◽

Peroxidase Gene

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Characterization of extracellular acid phosphatases from the yeast Arxula adeninivorans

Zentralblatt für Mikrobiologie ◽

10.1016/s0232-4393(11)80265-9 ◽

1991 ◽

Vol 146 (6) ◽

pp. 399-406 ◽

Cited By ~ 10

Author(s):

R. Büttner ◽

R. Bode ◽

D. Birnbaum

Keyword(s):

Arxula Adeninivorans ◽

Acid Phosphatases

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Characterization of a Maltase from an Early-Diverged Non-Conventional Yeast Blastobotrys adeninivorans

International Journal of Molecular Sciences ◽

10.3390/ijms21010297 ◽

2019 ◽

Vol 21 (1) ◽

pp. 297 ◽

Cited By ~ 1

Author(s):

Triinu Visnapuu ◽

Aivar Meldre ◽

Kristina Põšnograjeva ◽

Katrin Viigand ◽

Karin Ernits ◽

...

Keyword(s):

Escherichia Coli ◽

Saccharomyces Cerevisiae ◽

Aspergillus Oryzae ◽

Hydrolysis Product ◽

Hydrolytic Activity ◽

Glycoside Hydrolases ◽

Arxula Adeninivorans ◽

Sequence Identity ◽

Diabetes Drug

Genome of an early-diverged yeast Blastobotrys (Arxula) adeninivorans (Ba) encodes 88 glycoside hydrolases (GHs) including two α-glucosidases of GH13 family. One of those, the rna_ARAD1D20130g-encoded protein (BaAG2; 581 aa) was overexpressed in Escherichia coli, purified and characterized. We showed that maltose, other maltose-like substrates (maltulose, turanose, maltotriose, melezitose, malto-oligosaccharides of DP 4‒7) and sucrose were hydrolyzed by BaAG2, whereas isomaltose and isomaltose-like substrates (palatinose, α-methylglucoside) were not, confirming that BaAG2 is a maltase. BaAG2 was competitively inhibited by a diabetes drug acarbose (Ki = 0.8 µM) and Tris (Ki = 70.5 µM). BaAG2 was competitively inhibited also by isomaltose-like sugars and a hydrolysis product—glucose. At high maltose concentrations, BaAG2 exhibited transglycosylating ability producing potentially prebiotic di- and trisaccharides. Atypically for yeast maltases, a low but clearly recordable exo-hydrolytic activity on amylose, amylopectin and glycogen was detected. Saccharomyces cerevisiae maltase MAL62, studied for comparison, had only minimal ability to hydrolyze these polymers, and its transglycosylating activity was about three times lower compared to BaAG2. Sequence identity of BaAG2 with other maltases was only moderate being the highest (51%) with the maltase MalT of Aspergillus oryzae.

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