{"title":"丝状真菌里氏木霉漆酶活性的研究","authors":"Semra Sekme, N. Ataci, Inci Arisan","doi":"10.18478/IUFSJB.50042","DOIUrl":null,"url":null,"abstract":"Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source.","PeriodicalId":14521,"journal":{"name":"IUFS Journal of Biology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":"{\"title\":\"Studies on Laccase Activity in the Filamentous Fungus Trichoderma reesei\",\"authors\":\"Semra Sekme, N. Ataci, Inci Arisan\",\"doi\":\"10.18478/IUFSJB.50042\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source.\",\"PeriodicalId\":14521,\"journal\":{\"name\":\"IUFS Journal of Biology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"IUFS Journal of Biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.18478/IUFSJB.50042\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"IUFS Journal of Biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.18478/IUFSJB.50042","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5
摘要
漆酶的研究主要集中在担子菌科的木腐真菌中,特别是在白腐真菌中。对其他真菌科的研究在很大程度上缺乏。本研究在以儿茶酚为基础的培养基中评价了里氏木霉漆酶的活性。结果表明,青苔漆酶在酸性pH范围内具有活性,最适pH为4.5。在含10 gL -1儿茶酚的培养基中,漆酶的活性为1.22 U ml -1,比含10 gL -1葡萄糖的培养基高6倍以上。同时测定了不同儿茶酚浓度下的漆酶活性。在15 gL -1浓度下,漆酶活性略有下降,最大活性为1.1 Uml -1。结果表明,在以儿茶酚为碳源的培养基中,灰杉漆酶活性高于葡萄糖。漆酶的研究主要集中在担子菌科的木腐真菌中,特别是在白腐真菌中。对其他真菌科的研究在很大程度上缺乏。本研究在以儿茶酚为基础的培养基中评价了里氏木霉漆酶的活性。结果表明,青苔漆酶在酸性pH范围内具有活性,最适pH为4.5。在含10 gL -1儿茶酚的培养基中,漆酶的活性为1.22 U ml -1,比含10 gL -1葡萄糖的培养基高6倍以上。同时测定了不同儿茶酚浓度下的漆酶活性。在15 gL -1浓度下,漆酶活性略有下降,最大活性为1.1 Uml -1。结果表明,在以儿茶酚为碳源的培养基中,灰杉漆酶活性高于葡萄糖。漆酶的研究主要集中在担子菌科的木腐真菌中,特别是在白腐真菌中。对其他真菌科的研究在很大程度上缺乏。本研究在以儿茶酚为基础的培养基中评价了里氏木霉漆酶的活性。结果表明,青苔漆酶在酸性pH范围内具有活性,最适pH为4.5。在含10 gL -1儿茶酚的培养基中,漆酶的活性为1.22 U ml -1,比含10 gL -1葡萄糖的培养基高6倍以上。同时测定了不同儿茶酚浓度下的漆酶活性。在15 gL -1浓度下,漆酶活性略有下降,最大活性为1.1 Uml -1。结果表明,在以儿茶酚为碳源的培养基中,灰杉漆酶活性高于葡萄糖。漆酶的研究主要集中在担子菌科的木腐真菌中,特别是在白腐真菌中。对其他真菌科的研究在很大程度上缺乏。本研究在以儿茶酚为基础的培养基中评价了里氏木霉漆酶的活性。结果表明,青苔漆酶在酸性pH范围内具有活性,最适pH为4.5。在含10 gL -1儿茶酚的培养基中,漆酶的活性为1.22 U ml -1,比含10 gL -1葡萄糖的培养基高6倍以上。同时测定了不同儿茶酚浓度下的漆酶活性。在15 gL -1浓度下,漆酶活性略有下降,最大活性为1.1 Uml -1。结果表明,在以儿茶酚为碳源的培养基中,灰杉漆酶活性高于葡萄糖。
Studies on Laccase Activity in the Filamentous Fungus Trichoderma reesei
Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source. Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especially in white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccase activity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme from T.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature of laccase from T. reesei was also 27 0 C. Laccase activity in medium containing 10 gL -1 catechol was 1.22 U ml -1 , which was more than 6 times higher than in medium containing 10 gL -1 glucose. Laccase activity of T.reesei was also determined in different catechol concentrations. At a concentration of 15 gL -1 , laccase activity slightly decreased and the obtained maximum activity was 1.1 Uml -1 . Laccase activity of T. reesei was found higher than glucose, in the medium containing catechol as carbon source.