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Transformation of humic acids by two-domain laccase from Streptomyces anulatus
[Display omitted] •The gene of two-domain laccase was cloned from the genome of Streptomyces anulatus•The enzyme was expressed and its properties were studied•Two-domain laccase is able to transform of humic compounds at alkaline pH The properties of two-domain laccase of Streptomyces anulatus (SaSL...
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| Published in: | Process biochemistry (1991) 2019-01, Vol.76, p.128-135 |
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| cited_by | cdi_FETCH-LOGICAL-c374t-b38e7cb954236dc378283aac8cfa785c60dd886107c055cfa316f0f2b77dc6923 |
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| cites | cdi_FETCH-LOGICAL-c374t-b38e7cb954236dc378283aac8cfa785c60dd886107c055cfa316f0f2b77dc6923 |
| container_end_page | 135 |
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| container_title | Process biochemistry (1991) |
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| creator | Lisov, A.V. Trubitsina, L.I. Lisova, Z.A. Trubitsin, I.V. Zavarzina, A.G. Leontievsky, A.A. |
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•The gene of two-domain laccase was cloned from the genome of Streptomyces anulatus•The enzyme was expressed and its properties were studied•Two-domain laccase is able to transform of humic compounds at alkaline pH
The properties of two-domain laccase of Streptomyces anulatus (SaSL) and its role in transformation of humic acids (HA) from chernozem, sod-podzolic soil and peat at alkaline pH values were studied. The SaSL was cloned, expressed in E. coli and obtained in an electrophoretically homogeneous state. SaSL is an oligomeric protein with a molecular weight of 235-300 kDa and six or eight subunits in the molecule. The molecular weight of the subunit is 37.7 kDa. Its catalytic properties are similar to those of the previously described two-domain laccase. The enzyme catalyzed oxidation of electron donors (K4[Fe(CN)6], ABTS) at acidic pH and phenolic substrates (2-methoxyphenol, 2,6-dimethixyphenol) at alkaline pH values. The efficiency of catalysis was higher in the case of electron donors than phenolic substrates. The enzyme showed a high thermal stability and was more stable at neutral and alkaline pH values. The enzyme effectively transformed humic acids at alkaline pH values. It was found that polymerization reactions took place during interaction of SaSL with HA, as well as with their high-molecular weight (>80 kDa) and low-molecular weight ( |
| doi_str_mv | 10.1016/j.procbio.2018.11.001 |
| format | article |
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•The gene of two-domain laccase was cloned from the genome of Streptomyces anulatus•The enzyme was expressed and its properties were studied•Two-domain laccase is able to transform of humic compounds at alkaline pH
The properties of two-domain laccase of Streptomyces anulatus (SaSL) and its role in transformation of humic acids (HA) from chernozem, sod-podzolic soil and peat at alkaline pH values were studied. The SaSL was cloned, expressed in E. coli and obtained in an electrophoretically homogeneous state. SaSL is an oligomeric protein with a molecular weight of 235-300 kDa and six or eight subunits in the molecule. The molecular weight of the subunit is 37.7 kDa. Its catalytic properties are similar to those of the previously described two-domain laccase. The enzyme catalyzed oxidation of electron donors (K4[Fe(CN)6], ABTS) at acidic pH and phenolic substrates (2-methoxyphenol, 2,6-dimethixyphenol) at alkaline pH values. The efficiency of catalysis was higher in the case of electron donors than phenolic substrates. The enzyme showed a high thermal stability and was more stable at neutral and alkaline pH values. The enzyme effectively transformed humic acids at alkaline pH values. It was found that polymerization reactions took place during interaction of SaSL with HA, as well as with their high-molecular weight (>80 kDa) and low-molecular weight (<5 kDa) fractions. Our results suggest a possible involvement of the two-domaim laccases in humification processes in alkaline soils.</description><identifier>ISSN: 1359-5113</identifier><identifier>EISSN: 1873-3298</identifier><identifier>DOI: 10.1016/j.procbio.2018.11.001</identifier><language>eng</language><publisher>Barking: Elsevier Ltd</publisher><subject>Acidic oxides ; Alkaline soils ; Catalysis ; E coli ; Enzymes ; Humic acids ; Humic acids transformation ; Humic substances ; Humification ; Laccase ; Molecular weight ; Oxidation ; Peat ; pH effects ; Phenols ; Podzolic soils ; Polymerization ; Proteins ; Streptomyces ; Streptomyces anulatus ; Substrates ; Thermal stability</subject><ispartof>Process biochemistry (1991), 2019-01, Vol.76, p.128-135</ispartof><rights>2018 Elsevier Ltd</rights><rights>Copyright Elsevier BV Jan 2019</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c374t-b38e7cb954236dc378283aac8cfa785c60dd886107c055cfa316f0f2b77dc6923</citedby><cites>FETCH-LOGICAL-c374t-b38e7cb954236dc378283aac8cfa785c60dd886107c055cfa316f0f2b77dc6923</cites><orcidid>0000-0002-0682-0224 ; 0000-0002-6483-945X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Lisov, A.V.</creatorcontrib><creatorcontrib>Trubitsina, L.I.</creatorcontrib><creatorcontrib>Lisova, Z.A.</creatorcontrib><creatorcontrib>Trubitsin, I.V.</creatorcontrib><creatorcontrib>Zavarzina, A.G.</creatorcontrib><creatorcontrib>Leontievsky, A.A.</creatorcontrib><title>Transformation of humic acids by two-domain laccase from Streptomyces anulatus</title><title>Process biochemistry (1991)</title><description>[Display omitted]
•The gene of two-domain laccase was cloned from the genome of Streptomyces anulatus•The enzyme was expressed and its properties were studied•Two-domain laccase is able to transform of humic compounds at alkaline pH
The properties of two-domain laccase of Streptomyces anulatus (SaSL) and its role in transformation of humic acids (HA) from chernozem, sod-podzolic soil and peat at alkaline pH values were studied. The SaSL was cloned, expressed in E. coli and obtained in an electrophoretically homogeneous state. SaSL is an oligomeric protein with a molecular weight of 235-300 kDa and six or eight subunits in the molecule. The molecular weight of the subunit is 37.7 kDa. Its catalytic properties are similar to those of the previously described two-domain laccase. The enzyme catalyzed oxidation of electron donors (K4[Fe(CN)6], ABTS) at acidic pH and phenolic substrates (2-methoxyphenol, 2,6-dimethixyphenol) at alkaline pH values. The efficiency of catalysis was higher in the case of electron donors than phenolic substrates. The enzyme showed a high thermal stability and was more stable at neutral and alkaline pH values. The enzyme effectively transformed humic acids at alkaline pH values. It was found that polymerization reactions took place during interaction of SaSL with HA, as well as with their high-molecular weight (>80 kDa) and low-molecular weight (<5 kDa) fractions. Our results suggest a possible involvement of the two-domaim laccases in humification processes in alkaline soils.</description><subject>Acidic oxides</subject><subject>Alkaline soils</subject><subject>Catalysis</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Humic acids</subject><subject>Humic acids transformation</subject><subject>Humic substances</subject><subject>Humification</subject><subject>Laccase</subject><subject>Molecular weight</subject><subject>Oxidation</subject><subject>Peat</subject><subject>pH effects</subject><subject>Phenols</subject><subject>Podzolic soils</subject><subject>Polymerization</subject><subject>Proteins</subject><subject>Streptomyces</subject><subject>Streptomyces anulatus</subject><subject>Substrates</subject><subject>Thermal stability</subject><issn>1359-5113</issn><issn>1873-3298</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNqFkE9LAzEQxRdRsFY_ghDwvGsm6W6yJ5HiPyh6sJ5DdjbBlO6mJlml396Uevc0w-O9N8yvKK6BVkChud1Uu-Cxc75iFGQFUFEKJ8UMpOAlZ608zTuv27IG4OfFRYwbSjkA0Fnxug56jNaHQSfnR-It-ZwGh0Sj6yPp9iT9-LL3g3Yj2WpEHQ2xwQ_kPQWzS37Yo4lEj9NWpyleFmdWb6O5-pvz4uPxYb18LldvTy_L-1WJXCxS2XFpBHZtvWC86bMmmeRao0SrhayxoX0vZQNUIK3rLHJoLLWsE6LHpmV8Xtwce_PnX5OJSW38FMZ8UjEQElgNLWRXfXRh8DEGY9UuuEGHvQKqDujURv2hUwd0CkBldDl3d8yZ_MK3M0FFdGZE07tgMKneu38afgE1v3qo</recordid><startdate>201901</startdate><enddate>201901</enddate><creator>Lisov, A.V.</creator><creator>Trubitsina, L.I.</creator><creator>Lisova, Z.A.</creator><creator>Trubitsin, I.V.</creator><creator>Zavarzina, A.G.</creator><creator>Leontievsky, A.A.</creator><general>Elsevier Ltd</general><general>Elsevier BV</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><orcidid>https://orcid.org/0000-0002-0682-0224</orcidid><orcidid>https://orcid.org/0000-0002-6483-945X</orcidid></search><sort><creationdate>201901</creationdate><title>Transformation of humic acids by two-domain laccase from Streptomyces anulatus</title><author>Lisov, A.V. ; Trubitsina, L.I. ; Lisova, Z.A. ; Trubitsin, I.V. ; Zavarzina, A.G. ; Leontievsky, A.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c374t-b38e7cb954236dc378283aac8cfa785c60dd886107c055cfa316f0f2b77dc6923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Acidic oxides</topic><topic>Alkaline soils</topic><topic>Catalysis</topic><topic>E coli</topic><topic>Enzymes</topic><topic>Humic acids</topic><topic>Humic acids transformation</topic><topic>Humic substances</topic><topic>Humification</topic><topic>Laccase</topic><topic>Molecular weight</topic><topic>Oxidation</topic><topic>Peat</topic><topic>pH effects</topic><topic>Phenols</topic><topic>Podzolic soils</topic><topic>Polymerization</topic><topic>Proteins</topic><topic>Streptomyces</topic><topic>Streptomyces anulatus</topic><topic>Substrates</topic><topic>Thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lisov, A.V.</creatorcontrib><creatorcontrib>Trubitsina, L.I.</creatorcontrib><creatorcontrib>Lisova, Z.A.</creatorcontrib><creatorcontrib>Trubitsin, I.V.</creatorcontrib><creatorcontrib>Zavarzina, A.G.</creatorcontrib><creatorcontrib>Leontievsky, A.A.</creatorcontrib><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Process biochemistry (1991)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lisov, A.V.</au><au>Trubitsina, L.I.</au><au>Lisova, Z.A.</au><au>Trubitsin, I.V.</au><au>Zavarzina, A.G.</au><au>Leontievsky, A.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transformation of humic acids by two-domain laccase from Streptomyces anulatus</atitle><jtitle>Process biochemistry (1991)</jtitle><date>2019-01</date><risdate>2019</risdate><volume>76</volume><spage>128</spage><epage>135</epage><pages>128-135</pages><issn>1359-5113</issn><eissn>1873-3298</eissn><abstract>[Display omitted]
•The gene of two-domain laccase was cloned from the genome of Streptomyces anulatus•The enzyme was expressed and its properties were studied•Two-domain laccase is able to transform of humic compounds at alkaline pH
The properties of two-domain laccase of Streptomyces anulatus (SaSL) and its role in transformation of humic acids (HA) from chernozem, sod-podzolic soil and peat at alkaline pH values were studied. The SaSL was cloned, expressed in E. coli and obtained in an electrophoretically homogeneous state. SaSL is an oligomeric protein with a molecular weight of 235-300 kDa and six or eight subunits in the molecule. The molecular weight of the subunit is 37.7 kDa. Its catalytic properties are similar to those of the previously described two-domain laccase. The enzyme catalyzed oxidation of electron donors (K4[Fe(CN)6], ABTS) at acidic pH and phenolic substrates (2-methoxyphenol, 2,6-dimethixyphenol) at alkaline pH values. The efficiency of catalysis was higher in the case of electron donors than phenolic substrates. The enzyme showed a high thermal stability and was more stable at neutral and alkaline pH values. The enzyme effectively transformed humic acids at alkaline pH values. It was found that polymerization reactions took place during interaction of SaSL with HA, as well as with their high-molecular weight (>80 kDa) and low-molecular weight (<5 kDa) fractions. Our results suggest a possible involvement of the two-domaim laccases in humification processes in alkaline soils.</abstract><cop>Barking</cop><pub>Elsevier Ltd</pub><doi>10.1016/j.procbio.2018.11.001</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-0682-0224</orcidid><orcidid>https://orcid.org/0000-0002-6483-945X</orcidid></addata></record> |
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| ispartof | Process biochemistry (1991), 2019-01, Vol.76, p.128-135 |
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| subjects | Acidic oxides Alkaline soils Catalysis E coli Enzymes Humic acids Humic acids transformation Humic substances Humification Laccase Molecular weight Oxidation Peat pH effects Phenols Podzolic soils Polymerization Proteins Streptomyces Streptomyces anulatus Substrates Thermal stability |
| title | Transformation of humic acids by two-domain laccase from Streptomyces anulatus |
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