Solubilization of low-rank coal by Trichoderma atroviride: Evidence for the involvement of hydrolytic and oxidative enzymes by using 14C-labelled lignite
The deuteromycete Trichoderma atroviride is able to solubilize lignite in dependence on a given carbon source for growth. When cultivated on media containing glutamate, this mold excreted a set of different enzymes with hydrolytic activity. Addition of lignite to the growth media induced the synthes...
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Veröffentlicht in: | Journal of industrial microbiology & biotechnology 2002-04, Vol.28 (4), p.207-212 |
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creator | HÖLKER, U SCHMIERS, H GROSSE, S WINKELHÖFER, M POLSAKIEWICZ, M LUDWIG, S DOHSE, J HÖFER, M |
description | The deuteromycete Trichoderma atroviride is able to solubilize lignite in dependence on a given carbon source for growth. When cultivated on media containing glutamate, this mold excreted a set of different enzymes with hydrolytic activity. Addition of lignite to the growth media induced the synthesis of extracellular lignite-specific esterase activity but no evidence has been provided for its direct involvement in the process of lignite solubilization. Hence, the basic capability of T. atroviride enzymes to degrade a variety of ester and ether bonds at the surface or within the bulky lignite structure was tested using coal following its direct labelling with 14C-alkyl iodide. The participation of hydrolytic and oxidative enzymes in lignite degradation was assessed by measuring the release of 14C radioactivity from selectively alkylated carboxylic and phenolic OH groups. T. atroviride cleaved both carboxylic esters using esterases and the phenolic ether bonds by using oxidative enzymes, most likely laccases. |
doi_str_mv | 10.1038/sj/jim/7000232 |
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When cultivated on media containing glutamate, this mold excreted a set of different enzymes with hydrolytic activity. Addition of lignite to the growth media induced the synthesis of extracellular lignite-specific esterase activity but no evidence has been provided for its direct involvement in the process of lignite solubilization. Hence, the basic capability of T. atroviride enzymes to degrade a variety of ester and ether bonds at the surface or within the bulky lignite structure was tested using coal following its direct labelling with 14C-alkyl iodide. The participation of hydrolytic and oxidative enzymes in lignite degradation was assessed by measuring the release of 14C radioactivity from selectively alkylated carboxylic and phenolic OH groups. T. atroviride cleaved both carboxylic esters using esterases and the phenolic ether bonds by using oxidative enzymes, most likely laccases.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1038/sj/jim/7000232</identifier><identifier>PMID: 11986921</identifier><language>eng</language><publisher>Heidelberg: Springer</publisher><subject>Acids ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Carbon ; Carbon Radioisotopes ; Carbon sources ; Cellular biology ; Coal ; Coal - microbiology ; Enzymes ; Esterases - metabolism ; Esters ; Fundamental and applied biological sciences. Psychology ; Fungi ; Growth media ; Investigations ; Iodides ; Laccase ; Lignin ; Lignite ; Microbiology ; Microorganisms ; Mission oriented research ; Oxidoreductases - metabolism ; Phenols ; Physiology and metabolism ; Radioactivity ; Solubility ; Spectroscopy, Fourier Transform Infrared ; Studies ; Trichoderma - enzymology</subject><ispartof>Journal of industrial microbiology & biotechnology, 2002-04, Vol.28 (4), p.207-212</ispartof><rights>2002 INIST-CNRS</rights><rights>Society for Industrial Microbiology 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13613225$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11986921$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HÖLKER, U</creatorcontrib><creatorcontrib>SCHMIERS, H</creatorcontrib><creatorcontrib>GROSSE, S</creatorcontrib><creatorcontrib>WINKELHÖFER, M</creatorcontrib><creatorcontrib>POLSAKIEWICZ, M</creatorcontrib><creatorcontrib>LUDWIG, S</creatorcontrib><creatorcontrib>DOHSE, J</creatorcontrib><creatorcontrib>HÖFER, M</creatorcontrib><title>Solubilization of low-rank coal by Trichoderma atroviride: Evidence for the involvement of hydrolytic and oxidative enzymes by using 14C-labelled lignite</title><title>Journal of industrial microbiology & biotechnology</title><addtitle>J Ind Microbiol Biotechnol</addtitle><description>The deuteromycete Trichoderma atroviride is able to solubilize lignite in dependence on a given carbon source for growth. When cultivated on media containing glutamate, this mold excreted a set of different enzymes with hydrolytic activity. Addition of lignite to the growth media induced the synthesis of extracellular lignite-specific esterase activity but no evidence has been provided for its direct involvement in the process of lignite solubilization. Hence, the basic capability of T. atroviride enzymes to degrade a variety of ester and ether bonds at the surface or within the bulky lignite structure was tested using coal following its direct labelling with 14C-alkyl iodide. The participation of hydrolytic and oxidative enzymes in lignite degradation was assessed by measuring the release of 14C radioactivity from selectively alkylated carboxylic and phenolic OH groups. T. atroviride cleaved both carboxylic esters using esterases and the phenolic ether bonds by using oxidative enzymes, most likely laccases.</description><subject>Acids</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Carbon</subject><subject>Carbon Radioisotopes</subject><subject>Carbon sources</subject><subject>Cellular biology</subject><subject>Coal</subject><subject>Coal - microbiology</subject><subject>Enzymes</subject><subject>Esterases - metabolism</subject><subject>Esters</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungi</subject><subject>Growth media</subject><subject>Investigations</subject><subject>Iodides</subject><subject>Laccase</subject><subject>Lignin</subject><subject>Lignite</subject><subject>Microbiology</subject><subject>Microorganisms</subject><subject>Mission oriented research</subject><subject>Oxidoreductases - metabolism</subject><subject>Phenols</subject><subject>Physiology and metabolism</subject><subject>Radioactivity</subject><subject>Solubility</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Studies</subject><subject>Trichoderma - enzymology</subject><issn>1367-5435</issn><issn>1476-5535</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkE2LFDEQhoMo7jp69ShB0Fs7-ZgkHW8yrB-w4MH13KST6p2M6WRMult7_4n_1iyOCNblrcPDU8WL0HNK3lDC2205bo9-3CpCCOPsAbqkOyUbIbh4WHcuVSN2XFygJ6UcKyOUYo_RBaW6lZrRS_TrSwpz74O_M5NPEacBh_SjySZ-wzaZgPsV32RvD8lBHg02U06Lz97BW3y11IgW8JAyng6AfVxSWGCEON2LDqvLKayTt9hEh9NP7-qRBTDEu3WEcu-ei4-3mO72TTA9hAAOB38b_QRP0aPBhALPzrlBX99f3ew_NtefP3zav7tuTrROo5kcWm4NY0PrKNfOKqXdYAVIpgkTauDEWdlTLRgBCVqCkVIQzdVADQi-Qa__eE85fZ-hTN3oi62vmAhpLp2icieE5BV8-R94THOO9bdOVR9RbZVu0IszNPcjuO6U_Wjy2v1tvAKvzoAp1oShNm19-cdxSTljgv8G1RWR8w</recordid><startdate>200204</startdate><enddate>200204</enddate><creator>HÖLKER, U</creator><creator>SCHMIERS, H</creator><creator>GROSSE, S</creator><creator>WINKELHÖFER, M</creator><creator>POLSAKIEWICZ, M</creator><creator>LUDWIG, S</creator><creator>DOHSE, J</creator><creator>HÖFER, M</creator><general>Springer</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>200204</creationdate><title>Solubilization of low-rank coal by Trichoderma atroviride: Evidence for the involvement of hydrolytic and oxidative enzymes by using 14C-labelled lignite</title><author>HÖLKER, U ; SCHMIERS, H ; GROSSE, S ; WINKELHÖFER, M ; POLSAKIEWICZ, M ; LUDWIG, S ; DOHSE, J ; HÖFER, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1111-926f83ca22f8d139dc779dfc5e6290257f30dc6b19520e6e96ea6650937f1ae53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Acids</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Carbon</topic><topic>Carbon Radioisotopes</topic><topic>Carbon sources</topic><topic>Cellular biology</topic><topic>Coal</topic><topic>Coal - microbiology</topic><topic>Enzymes</topic><topic>Esterases - metabolism</topic><topic>Esters</topic><topic>Fundamental and applied biological sciences. 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Academic</collection><jtitle>Journal of industrial microbiology & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HÖLKER, U</au><au>SCHMIERS, H</au><au>GROSSE, S</au><au>WINKELHÖFER, M</au><au>POLSAKIEWICZ, M</au><au>LUDWIG, S</au><au>DOHSE, J</au><au>HÖFER, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solubilization of low-rank coal by Trichoderma atroviride: Evidence for the involvement of hydrolytic and oxidative enzymes by using 14C-labelled lignite</atitle><jtitle>Journal of industrial microbiology & biotechnology</jtitle><addtitle>J Ind Microbiol Biotechnol</addtitle><date>2002-04</date><risdate>2002</risdate><volume>28</volume><issue>4</issue><spage>207</spage><epage>212</epage><pages>207-212</pages><issn>1367-5435</issn><eissn>1476-5535</eissn><abstract>The deuteromycete Trichoderma atroviride is able to solubilize lignite in dependence on a given carbon source for growth. When cultivated on media containing glutamate, this mold excreted a set of different enzymes with hydrolytic activity. Addition of lignite to the growth media induced the synthesis of extracellular lignite-specific esterase activity but no evidence has been provided for its direct involvement in the process of lignite solubilization. Hence, the basic capability of T. atroviride enzymes to degrade a variety of ester and ether bonds at the surface or within the bulky lignite structure was tested using coal following its direct labelling with 14C-alkyl iodide. The participation of hydrolytic and oxidative enzymes in lignite degradation was assessed by measuring the release of 14C radioactivity from selectively alkylated carboxylic and phenolic OH groups. T. atroviride cleaved both carboxylic esters using esterases and the phenolic ether bonds by using oxidative enzymes, most likely laccases.</abstract><cop>Heidelberg</cop><pub>Springer</pub><pmid>11986921</pmid><doi>10.1038/sj/jim/7000232</doi><tpages>6</tpages></addata></record> |
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subjects | Acids Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Carbon Carbon Radioisotopes Carbon sources Cellular biology Coal Coal - microbiology Enzymes Esterases - metabolism Esters Fundamental and applied biological sciences. Psychology Fungi Growth media Investigations Iodides Laccase Lignin Lignite Microbiology Microorganisms Mission oriented research Oxidoreductases - metabolism Phenols Physiology and metabolism Radioactivity Solubility Spectroscopy, Fourier Transform Infrared Studies Trichoderma - enzymology |
title | Solubilization of low-rank coal by Trichoderma atroviride: Evidence for the involvement of hydrolytic and oxidative enzymes by using 14C-labelled lignite |
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