Loading…

Cellulase Formation by Species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with Anamorphs Referable toTrichodermasect.Longibrachiatum

Kubicek, C. P., Bölzlbauer, U.M., Kovacs, W., Mach, R. L., Kuhls, K., Lieckfeldt, E., Börner, T., and Samuels, G. J. 1996. Cellulase formation by species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with anamorphs referable toTrichodermasect.Longibrachiatum. Fungal Genetics and Biology20,105–...

Full description

Saved in:
Bibliographic Details
Published in:Fungal genetics and biology 1996-06, Vol.20 (2), p.105-114
Main Authors: Kubicek, Christian P., Bölzlbauer, Ulrike M., Kovacs, Werner, Mach, Robert L., Kuhls, Katrin, Lieckfeldt, Elke, Börner, Thomas, Samuels, Gary J.
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c1335-5d6754670eeafbaaeac8cc030bff5eb6d401708465dd7ea4bda3a2625706421c3
cites
container_end_page 114
container_issue 2
container_start_page 105
container_title Fungal genetics and biology
container_volume 20
creator Kubicek, Christian P.
Bölzlbauer, Ulrike M.
Kovacs, Werner
Mach, Robert L.
Kuhls, Katrin
Lieckfeldt, Elke
Börner, Thomas
Samuels, Gary J.
description Kubicek, C. P., Bölzlbauer, U.M., Kovacs, W., Mach, R. L., Kuhls, K., Lieckfeldt, E., Börner, T., and Samuels, G. J. 1996. Cellulase formation by species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with anamorphs referable toTrichodermasect.Longibrachiatum. Fungal Genetics and Biology20,105–114. The cellulolytic potential of the wild-type strain ofTrichoderma reeseiwas compared to other members ofTrichodermasect.LongibrachiatumandHypocreaspp. that have anamorphs referable to that section. There was high diversity even within the same species (as defined by morphological and macromolecular characters). Differences, where notable, were more pronounced for carboxymethyl-cellulase activity than for filter paper activity. High cellulase activities were observed for several strains ofT. longibrachiatumandT. citrinoviride,whereasT. parceramosumformed only low levels of activity. Among the corresponding teleomorphs, most strains ofH. schweinitziiwere comparatively poor producers, whereas the highest percentage of high producers was found amongH. jecorinaisolates, and many strains were even more active than the parentT. reeseiQM 6a. Immunoblot analysis of corresponding culture filtrates of variousH. jecorinastrains showed that the three major cellulase proteins (cellobiohydrolase I, cellobiohydrolase II, and endoglucanase I) were present in culture filtrates and theirMrwas identical to that of the respectiveT. reeseiproteins. ELISA analysis demonstrated that these enzymes were also present in the same relative proportions in culture filtrates fromH. jecorinaandT. reesei.With the aid of primers, corresponding to conserved sequences in the cellobiohydrolase I-encoding genecbh1,a fragment of this gene was amplified from selected strains ofH. jecorina, T. reesei, T. longibrachiatum, T. citrinoviride,andH. schweinitzii.The fragments had the same size in all fungi. Cleavage of this fragment withHhaI produced a RFLP pattern which was identical inH. jecorinaandT. reesei,but different in the other species. In the latter, the RFLP pattern was also species specific. These results provide support for a close genetic similarity ofT. reeseiandH. jecorinacellulases. In the latter, an ascomycetous model system for cellulase biosynthesis is now availabale. The results further indicate that other anamorphs ofTrichodermasectionLongibrachiatumare promising sources of high cellulase production.
doi_str_mv 10.1006/fgbi.1996.0025
format article
fullrecord <record><control><sourceid>elsevier_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1006_fgbi_1996_0025</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1087184596900250</els_id><sourcerecordid>S1087184596900250</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1335-5d6754670eeafbaaeac8cc030bff5eb6d401708465dd7ea4bda3a2625706421c3</originalsourceid><addsrcrecordid>eNqFkMFKxDAQhoMouK5ePecFWpO2SdvjsriusCDoeg7TZLqNtE1Juso-hO9sy3oVTzMw8_3MfITccxZzxuRDfahszMtSxowl4oIsOCtlxMo0v5z7Io94kYlrchPCB2Oci4wvyPca2_bYQkC6cb6D0bqeVif6NqC2GKir997qxhmchgH1GO9cf7CVB91YGI8d9GZa2p4Gpz1CGIaYftmxoaseOueHJtBXrNFD1SId3T9ht-Sqhjbg3W9dkvfN4369jXYvT8_r1S7SPE1FJIzMRSZzhgh1BYCgC61Zyqq6FlhJkzGesyKTwpgcIasMpJDIRORMZgnX6ZLE51ztXQgeazV424E_Kc7ULFPNMtUsU80yJ6A4Azhd9WnRqzDp6TUa66c_lHH2L_QHFiyAlQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Cellulase Formation by Species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with Anamorphs Referable toTrichodermasect.Longibrachiatum</title><source>Elsevier</source><creator>Kubicek, Christian P. ; Bölzlbauer, Ulrike M. ; Kovacs, Werner ; Mach, Robert L. ; Kuhls, Katrin ; Lieckfeldt, Elke ; Börner, Thomas ; Samuels, Gary J.</creator><creatorcontrib>Kubicek, Christian P. ; Bölzlbauer, Ulrike M. ; Kovacs, Werner ; Mach, Robert L. ; Kuhls, Katrin ; Lieckfeldt, Elke ; Börner, Thomas ; Samuels, Gary J.</creatorcontrib><description>Kubicek, C. P., Bölzlbauer, U.M., Kovacs, W., Mach, R. L., Kuhls, K., Lieckfeldt, E., Börner, T., and Samuels, G. J. 1996. Cellulase formation by species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with anamorphs referable toTrichodermasect.Longibrachiatum. Fungal Genetics and Biology20,105–114. The cellulolytic potential of the wild-type strain ofTrichoderma reeseiwas compared to other members ofTrichodermasect.LongibrachiatumandHypocreaspp. that have anamorphs referable to that section. There was high diversity even within the same species (as defined by morphological and macromolecular characters). Differences, where notable, were more pronounced for carboxymethyl-cellulase activity than for filter paper activity. High cellulase activities were observed for several strains ofT. longibrachiatumandT. citrinoviride,whereasT. parceramosumformed only low levels of activity. Among the corresponding teleomorphs, most strains ofH. schweinitziiwere comparatively poor producers, whereas the highest percentage of high producers was found amongH. jecorinaisolates, and many strains were even more active than the parentT. reeseiQM 6a. Immunoblot analysis of corresponding culture filtrates of variousH. jecorinastrains showed that the three major cellulase proteins (cellobiohydrolase I, cellobiohydrolase II, and endoglucanase I) were present in culture filtrates and theirMrwas identical to that of the respectiveT. reeseiproteins. ELISA analysis demonstrated that these enzymes were also present in the same relative proportions in culture filtrates fromH. jecorinaandT. reesei.With the aid of primers, corresponding to conserved sequences in the cellobiohydrolase I-encoding genecbh1,a fragment of this gene was amplified from selected strains ofH. jecorina, T. reesei, T. longibrachiatum, T. citrinoviride,andH. schweinitzii.The fragments had the same size in all fungi. Cleavage of this fragment withHhaI produced a RFLP pattern which was identical inH. jecorinaandT. reesei,but different in the other species. In the latter, the RFLP pattern was also species specific. These results provide support for a close genetic similarity ofT. reeseiandH. jecorinacellulases. In the latter, an ascomycetous model system for cellulase biosynthesis is now availabale. The results further indicate that other anamorphs ofTrichodermasectionLongibrachiatumare promising sources of high cellulase production.</description><identifier>ISSN: 1087-1845</identifier><identifier>EISSN: 1096-0937</identifier><identifier>DOI: 10.1006/fgbi.1996.0025</identifier><language>eng</language><publisher>Elsevier Inc</publisher><subject>cellobiohydrolase ; cellulase ; Hypocrea ; RFLP ; Trichoderma ; Trichoderma reesei</subject><ispartof>Fungal genetics and biology, 1996-06, Vol.20 (2), p.105-114</ispartof><rights>1996 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1335-5d6754670eeafbaaeac8cc030bff5eb6d401708465dd7ea4bda3a2625706421c3</citedby></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>Kubicek, Christian P.</creatorcontrib><creatorcontrib>Bölzlbauer, Ulrike M.</creatorcontrib><creatorcontrib>Kovacs, Werner</creatorcontrib><creatorcontrib>Mach, Robert L.</creatorcontrib><creatorcontrib>Kuhls, Katrin</creatorcontrib><creatorcontrib>Lieckfeldt, Elke</creatorcontrib><creatorcontrib>Börner, Thomas</creatorcontrib><creatorcontrib>Samuels, Gary J.</creatorcontrib><title>Cellulase Formation by Species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with Anamorphs Referable toTrichodermasect.Longibrachiatum</title><title>Fungal genetics and biology</title><description>Kubicek, C. P., Bölzlbauer, U.M., Kovacs, W., Mach, R. L., Kuhls, K., Lieckfeldt, E., Börner, T., and Samuels, G. J. 1996. Cellulase formation by species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with anamorphs referable toTrichodermasect.Longibrachiatum. Fungal Genetics and Biology20,105–114. The cellulolytic potential of the wild-type strain ofTrichoderma reeseiwas compared to other members ofTrichodermasect.LongibrachiatumandHypocreaspp. that have anamorphs referable to that section. There was high diversity even within the same species (as defined by morphological and macromolecular characters). Differences, where notable, were more pronounced for carboxymethyl-cellulase activity than for filter paper activity. High cellulase activities were observed for several strains ofT. longibrachiatumandT. citrinoviride,whereasT. parceramosumformed only low levels of activity. Among the corresponding teleomorphs, most strains ofH. schweinitziiwere comparatively poor producers, whereas the highest percentage of high producers was found amongH. jecorinaisolates, and many strains were even more active than the parentT. reeseiQM 6a. Immunoblot analysis of corresponding culture filtrates of variousH. jecorinastrains showed that the three major cellulase proteins (cellobiohydrolase I, cellobiohydrolase II, and endoglucanase I) were present in culture filtrates and theirMrwas identical to that of the respectiveT. reeseiproteins. ELISA analysis demonstrated that these enzymes were also present in the same relative proportions in culture filtrates fromH. jecorinaandT. reesei.With the aid of primers, corresponding to conserved sequences in the cellobiohydrolase I-encoding genecbh1,a fragment of this gene was amplified from selected strains ofH. jecorina, T. reesei, T. longibrachiatum, T. citrinoviride,andH. schweinitzii.The fragments had the same size in all fungi. Cleavage of this fragment withHhaI produced a RFLP pattern which was identical inH. jecorinaandT. reesei,but different in the other species. In the latter, the RFLP pattern was also species specific. These results provide support for a close genetic similarity ofT. reeseiandH. jecorinacellulases. In the latter, an ascomycetous model system for cellulase biosynthesis is now availabale. The results further indicate that other anamorphs ofTrichodermasectionLongibrachiatumare promising sources of high cellulase production.</description><subject>cellobiohydrolase</subject><subject>cellulase</subject><subject>Hypocrea</subject><subject>RFLP</subject><subject>Trichoderma</subject><subject>Trichoderma reesei</subject><issn>1087-1845</issn><issn>1096-0937</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqFkMFKxDAQhoMouK5ePecFWpO2SdvjsriusCDoeg7TZLqNtE1Juso-hO9sy3oVTzMw8_3MfITccxZzxuRDfahszMtSxowl4oIsOCtlxMo0v5z7Io94kYlrchPCB2Oci4wvyPca2_bYQkC6cb6D0bqeVif6NqC2GKir997qxhmchgH1GO9cf7CVB91YGI8d9GZa2p4Gpz1CGIaYftmxoaseOueHJtBXrNFD1SId3T9ht-Sqhjbg3W9dkvfN4369jXYvT8_r1S7SPE1FJIzMRSZzhgh1BYCgC61Zyqq6FlhJkzGesyKTwpgcIasMpJDIRORMZgnX6ZLE51ztXQgeazV424E_Kc7ULFPNMtUsU80yJ6A4Azhd9WnRqzDp6TUa66c_lHH2L_QHFiyAlQ</recordid><startdate>199606</startdate><enddate>199606</enddate><creator>Kubicek, Christian P.</creator><creator>Bölzlbauer, Ulrike M.</creator><creator>Kovacs, Werner</creator><creator>Mach, Robert L.</creator><creator>Kuhls, Katrin</creator><creator>Lieckfeldt, Elke</creator><creator>Börner, Thomas</creator><creator>Samuels, Gary J.</creator><general>Elsevier Inc</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>199606</creationdate><title>Cellulase Formation by Species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with Anamorphs Referable toTrichodermasect.Longibrachiatum</title><author>Kubicek, Christian P. ; Bölzlbauer, Ulrike M. ; Kovacs, Werner ; Mach, Robert L. ; Kuhls, Katrin ; Lieckfeldt, Elke ; Börner, Thomas ; Samuels, Gary J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1335-5d6754670eeafbaaeac8cc030bff5eb6d401708465dd7ea4bda3a2625706421c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>cellobiohydrolase</topic><topic>cellulase</topic><topic>Hypocrea</topic><topic>RFLP</topic><topic>Trichoderma</topic><topic>Trichoderma reesei</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kubicek, Christian P.</creatorcontrib><creatorcontrib>Bölzlbauer, Ulrike M.</creatorcontrib><creatorcontrib>Kovacs, Werner</creatorcontrib><creatorcontrib>Mach, Robert L.</creatorcontrib><creatorcontrib>Kuhls, Katrin</creatorcontrib><creatorcontrib>Lieckfeldt, Elke</creatorcontrib><creatorcontrib>Börner, Thomas</creatorcontrib><creatorcontrib>Samuels, Gary J.</creatorcontrib><collection>CrossRef</collection><jtitle>Fungal genetics and biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kubicek, Christian P.</au><au>Bölzlbauer, Ulrike M.</au><au>Kovacs, Werner</au><au>Mach, Robert L.</au><au>Kuhls, Katrin</au><au>Lieckfeldt, Elke</au><au>Börner, Thomas</au><au>Samuels, Gary J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cellulase Formation by Species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with Anamorphs Referable toTrichodermasect.Longibrachiatum</atitle><jtitle>Fungal genetics and biology</jtitle><date>1996-06</date><risdate>1996</risdate><volume>20</volume><issue>2</issue><spage>105</spage><epage>114</epage><pages>105-114</pages><issn>1087-1845</issn><eissn>1096-0937</eissn><abstract>Kubicek, C. P., Bölzlbauer, U.M., Kovacs, W., Mach, R. L., Kuhls, K., Lieckfeldt, E., Börner, T., and Samuels, G. J. 1996. Cellulase formation by species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with anamorphs referable toTrichodermasect.Longibrachiatum. Fungal Genetics and Biology20,105–114. The cellulolytic potential of the wild-type strain ofTrichoderma reeseiwas compared to other members ofTrichodermasect.LongibrachiatumandHypocreaspp. that have anamorphs referable to that section. There was high diversity even within the same species (as defined by morphological and macromolecular characters). Differences, where notable, were more pronounced for carboxymethyl-cellulase activity than for filter paper activity. High cellulase activities were observed for several strains ofT. longibrachiatumandT. citrinoviride,whereasT. parceramosumformed only low levels of activity. Among the corresponding teleomorphs, most strains ofH. schweinitziiwere comparatively poor producers, whereas the highest percentage of high producers was found amongH. jecorinaisolates, and many strains were even more active than the parentT. reeseiQM 6a. Immunoblot analysis of corresponding culture filtrates of variousH. jecorinastrains showed that the three major cellulase proteins (cellobiohydrolase I, cellobiohydrolase II, and endoglucanase I) were present in culture filtrates and theirMrwas identical to that of the respectiveT. reeseiproteins. ELISA analysis demonstrated that these enzymes were also present in the same relative proportions in culture filtrates fromH. jecorinaandT. reesei.With the aid of primers, corresponding to conserved sequences in the cellobiohydrolase I-encoding genecbh1,a fragment of this gene was amplified from selected strains ofH. jecorina, T. reesei, T. longibrachiatum, T. citrinoviride,andH. schweinitzii.The fragments had the same size in all fungi. Cleavage of this fragment withHhaI produced a RFLP pattern which was identical inH. jecorinaandT. reesei,but different in the other species. In the latter, the RFLP pattern was also species specific. These results provide support for a close genetic similarity ofT. reeseiandH. jecorinacellulases. In the latter, an ascomycetous model system for cellulase biosynthesis is now availabale. The results further indicate that other anamorphs ofTrichodermasectionLongibrachiatumare promising sources of high cellulase production.</abstract><pub>Elsevier Inc</pub><doi>10.1006/fgbi.1996.0025</doi><tpages>10</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1087-1845
ispartof Fungal genetics and biology, 1996-06, Vol.20 (2), p.105-114
issn 1087-1845
1096-0937
language eng
recordid cdi_crossref_primary_10_1006_fgbi_1996_0025
source Elsevier
subjects cellobiohydrolase
cellulase
Hypocrea
RFLP
Trichoderma
Trichoderma reesei
title Cellulase Formation by Species ofTrichodermasect.Longibrachiatumand ofHypocreaspp. with Anamorphs Referable toTrichodermasect.Longibrachiatum
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T20%3A55%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-elsevier_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cellulase%20Formation%20by%20Species%20ofTrichodermasect.Longibrachiatumand%20ofHypocreaspp.%20with%20Anamorphs%20Referable%20toTrichodermasect.Longibrachiatum&rft.jtitle=Fungal%20genetics%20and%20biology&rft.au=Kubicek,%20Christian%20P.&rft.date=1996-06&rft.volume=20&rft.issue=2&rft.spage=105&rft.epage=114&rft.pages=105-114&rft.issn=1087-1845&rft.eissn=1096-0937&rft_id=info:doi/10.1006/fgbi.1996.0025&rft_dat=%3Celsevier_cross%3ES1087184596900250%3C/elsevier_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c1335-5d6754670eeafbaaeac8cc030bff5eb6d401708465dd7ea4bda3a2625706421c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true