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Production of xylanases, mannanases, and pectinases by the thermophilic fungus Thermomyces lanuginosus

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dc.contributor.author Puchart, V en
dc.contributor.author Katapodis, P en
dc.contributor.author Biely, P en
dc.contributor.author Kremnicky, L en
dc.contributor.author Christakopoulos, P en
dc.contributor.author Vrsanska, M en
dc.contributor.author Kekos, D en
dc.contributor.author MacRis, BJ en
dc.contributor.author Bhat, MK en
dc.date.accessioned 2014-03-01T01:15:05Z
dc.date.available 2014-03-01T01:15:05Z
dc.date.issued 1999 en
dc.identifier.issn 0141-0229 en
dc.identifier.uri https://dspace.lib.ntua.gr/xmlui/handle/123456789/13331
dc.subject β-mannanase en
dc.subject Arabinanase en
dc.subject Pectinolytic enzymes en
dc.subject Thermomyces lanuginosus en
dc.subject Xylanase en
dc.subject.classification Biotechnology & Applied Microbiology en
dc.subject.other Biodegradation en
dc.subject.other Fungi en
dc.subject.other Mannase en
dc.subject.other Pectinase en
dc.subject.other Thermophilic fungus en
dc.subject.other Xylanase en
dc.subject.other Enzymes en
dc.subject.other beta mannosidase en
dc.subject.other pectin en
dc.subject.other polygalacturonase en
dc.subject.other sugar en
dc.subject.other xylan en
dc.subject.other xylan endo 1,3 beta xylosidase en
dc.subject.other article en
dc.subject.other enzyme stability en
dc.subject.other enzyme synthesis en
dc.subject.other fungus en
dc.subject.other nonhuman en
dc.subject.other thermostability en
dc.subject.other Thermomyces lanuginosus en
dc.title Production of xylanases, mannanases, and pectinases by the thermophilic fungus Thermomyces lanuginosus en
heal.type journalArticle en
heal.identifier.primary 10.1016/S0141-0229(98)00132-X en
heal.identifier.secondary http://dx.doi.org/10.1016/S0141-0229(98)00132-X en
heal.language English en
heal.publicationDate 1999 en
heal.abstract A group of 17 strains of the thermophilic fungus Thermomyces lanuginosus was examined for the production of xylanases, β-mannanases, arabinanases, and pectinases. All strains were found to be xylanolytic, and several were proven to be outstanding producers of microbial xylanase on glucuronoxylan and corn cobs. The strains hyperproducing xylanase secreted low amounts of xylan-debranching enzymes and did not produce β-mannan and arabinan-degrading enzyme systems. Only the strains showing lower xylanase production exhibited a higher degree of xylan utilization and also the ability to produce a mannanolytic enzyme system. One of the mannanolytic strains was found to be capable of producing arabinan-degrading enzymes. This strain also showed the best production of pectinolytic enzymes during growth on citrus pectin or sugar beet pulp. Some of the strains have good potential for use as sources of important industrial enzymes of high thermal stability. Copyright (C) 1999 Elsevier Science Inc.A group of 17 strains of the thermophilic fungus Thermomyces lanuginosus was examined for the production of xylanases, β-mannanases, arabinanases, and pectinases. All strains were found to be xylanolytic, and several were proven to be outstanding producers of microbial xylanase on glucuronoxylan and corn cobs. The strains hyperproducing xylanase secreted low amounts of xylan-debranching enzymes and did not produce β-mannan and arabinan-degrading enzyme systems. Only the strains showing lower xylanase production exhibited a higher degree of xylan utilization and also the ability to produce a mannanolytic enzyme system. One of the mannanolytic strains was found to be capable of producing arabinan-degrading enzymes. This strain also showed the best production of pectinolytic enzymes during growth on citrus pectin or sugar beet pulp. Some of the strains have good potential for use as sources of important industrial enzymes of high thermal stability. en
heal.publisher Elsevier Science Inc, New York, NY, United States en
heal.journalName Enzyme and Microbial Technology en
dc.identifier.doi 10.1016/S0141-0229(98)00132-X en
dc.identifier.isi ISI:000078929100017 en
dc.identifier.volume 24 en
dc.identifier.issue 5-6 en
dc.identifier.spage 355 en
dc.identifier.epage 361 en


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