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Journals / IUFS Journal of Biology / 2013 / Cilt: 72 - Sayı: 2

Trichoderma reesei küf mantarında lakkaz aktivitesinin incelenmesi

Studies on laccase activity in the filamentous fungus Trichoderma reesei

Nese ATACİ
Inci ARİSAN
Semra SEKME
Pages
37–42
Publication Date
2022-10-18
DOI
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Results showed that laccase enzyme fromT.reesei was active in acidic pH range and that optimum pH was 4.5.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especiallyin white rot fungi.
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Key Findings & Data:Results showed that laccase enzyme fromT.reesei was active in acidic pH range and that optimum pH was 4.5.
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Conclusion & Impact:Laccase activityof T. reesei was found higher than glucose, in the medium containing catechol as carbon source.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

Laccase have been mainly studied in wood rot fungal species of the basidiomycetes family especiallyin white rot fungi. Studies in other fungal families are largely lacking. This study has evaluated laccaseactivity from Trichoderma reesei in catechol based medium. Results showed that laccase enzyme fromT.reesei was active in acidic pH range and that optimum pH was 4.5. The optimum temperature oflaccase from T. reesei was also 270C. Laccase activity in medium containing 10 gL -1 catechol was 1.22U ml-1 , which was more than 6 times higher than in medium containing 10 gL-1 glucose. Laccase activityof 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 activityof T. reesei was found higher than glucose, in the medium containing catechol as carbon source.

Özet

Basidiomycetes sınıfında bulunan beyaz çürükçül mantarlar en çok çalışılmış lakkaz üreten mantarlardır.Diğer mantar ailelerinde lakkaz enzimi ile ilgili araştırmalar büyük ölçüde eksiktir. Bu çalışmada,Trichoderma reesei küf mantarında ve kateşol içeren ortamda lakkaz aktivitesi incelendi. Deneyselçalışmadan elde edilen sonuçlara göre, Trichoderma reeseide lakkaz enziminin asidik pHda aktifolduğu gözlendi. Lakkaz enziminin optimum pHsı 4.5 olarak belirlendi. Trichoderma reeseide lakkazenziminin optimum sıcaklığı da 27ºColarak tespit edildi. 10 gL-1 kateşol içeren ortamda, Trichodermareeseide lakkaz enziminin aktivitesi 10gL-1 glukoz içeren ortama göre 6 kat daha fazla bulundu.Lakkaz aktivitesi 1,22 U ml-1 olarak belirlendi. Trichoderma reeseide lakkaz aktivitesi farklı kateşolkonsantrasyonları için de tespit edildi. 15gL-1 kateşol konsantrasyonunda lakkaz aktivitesinin azaldığıgözlendi. 15gL-1 kateşol konsantrasyonunda maksimum lakkaz aktivitesi 1,1 UmL-1 olarak belirlendi.

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Cite This Article

ATACİ, N., ARİSAN, I., SEKME, S. (2022). Trichoderma reesei küf mantarında lakkaz aktivitesinin incelenmesi. IUFS Journal of Biology, Cilt: 72 - Sayı: 2, 37–42. https://ajindex.com/articles/544017

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References (12)

  1. Assavanig A., Amornikitticharoen B., Ekpaisal N., Meevootisom V., Flegel T.W. (1992) Isolation characterization and function of laccase from Trichoderma. Applied Microbiology and Biotechnology 38: 198-202. Baldrian P. ( 2006) Funcal Laccases-Ocurrence and Properties. FEMS Microbiolology Re- views 30: 215-242.
  2. Bradford M.M. (1976) A rapid and sensetive method for detecting microgram amount of protein utilizing the principle of protein –dye binding. Analytical Biochemistry, 72: 248-254.
  3. Brijwani K., Rigdon A., Vadlani P.V. (2010) Fungal laccase: Production function and applications in food processing, Enzyme Research, DOI: 10.4061/2010/149748. Desai S.S., Nityanand C. (2011) Microbial Laccases and their applicatio: A review, Asian Journal of Biotechnology, 3: 98-124.
  4. Gochev V.K., Krastanov A.I. (2007) Isolation of Laccase Producing Trichodema Spp. Bulgarian Journal of Agriculture Science, 13: 171-176.
  5. Eggert C., Temp U., Dean J.F.D., Eriksson K.E.L. (1996) A fungal metabolite mediates degredation of nonphenolic lignin structures and synthetic lignin by laccase. FEBS Letters, 391: 144-148.
  6. Harman G.E., Herrera-Estrella A.H., Horwitz B.A., Lorito M. (2012) Special Issue: Trichoderma-from Basic Biology to Biotechnology. Microbiology, 158: 1-2.
  7. H ölker U., Dohse J., Höfer M. (2002) Extracellular laccases in ascomycetes Trichoderma atroviride and Trichoderma harzianum. Folia Microbiologica, 47: 423-427.
  8. Kahraman S.S., Gurdal I.H. (2002) Effect of synthetic and natural culture media on laccase production by white rot fungi, Bioresource Technology, 82: 215-217.
  9. Kunamneni A., Plou F.J., Ballesteros A., Alcalde M. (2008) Laccases and their applications: A Patent Review, Recent Patent on Biotechnology, 2: 10-24.
  10. Pazarlıoğlu N.K., Sarişik M., Telefoncu A. (2005) Laccase:Production by Trametes versicolor and Application to Denim Washing. Process Biochemistry, 40: 1673- 1678. Rigo M., Alegre R.M., Bezerra J.R.M.V., Coel- ho N., Bastos R.G. (2010) Catechol biodegredation kinetics using Candida parapsilosis. Brazillian Archive Biology and Technology,53: 481-486.
  11. Rodriguez C.S., Herrara F.L.T. (2006) Industrial and biotechological applications of laccase. Biotechnology Advances, 24: 500- 513. Thurston C.F. (1994) The structure and function of fungal laccases. Microbiology, 140: 19-26.
  12. Velazquez-Cedeno M.A., Farnet A.M., Ferre E &Savoie J.M. (2004) Variations of ligno- cellulosicactivities in dual cultures of pleurotus ostreatus and Trichoderma lon- gibrachiatum on unsteri