About Bioline  All Journals  Testimonials  Membership  News  Donations

Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 18, No. 6, 2015, pp. 1-7
Bioline Code: ej15065
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 18, No. 6, 2015, pp. 1-7

 en Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius check for this species in other resources produced under solid-state fermentation
Valera, Larissa Serrani; Jorge, João Atílio & Guimarães, Luis Henrique Souza


Background: Tannases are enzymes with biotechnological potential produced mainly by microorganisms as filamentous fungi. In this context, the production and characterization of a multi-tolerant tannase from Aspergillus carbonarius check for this species in other resources is described.
Results: The filamentous fungus A. carbonarius produced high levels of tannasewhen cultivated under solid-state fermentation using green tea leaves as substrate/carbon source and tapwater at a 1:1 ratio as the moisture agent for 72 h at 30°C. Two tannase activity peakswere obtained during the purification step usingDEAE-Cellulose. The second peak (peak II) was purified 11-fold with 14% recovery from a Sepharose CL-6B chromatographic column. The tannase frompeak II (tannase II)was characterized as a heterodimeric glycoprotein of 134.89 kDa, estimated through gel filtration,with subunits of 65 kDa and 100 kDa, estimated through SDS-PAGE, and 48% carbohydrate content. The optimal temperature and pH for tannase II activity was 60°C and 5.0, respectively. The enzyme was fully stable at temperatures ranging from 20–60°C for 120 min, and the half-life (T1/2) at 75°C was 62 min. The activation energy was 28.93 kJ/mol. After incubation at pH 5.0 for 60 min, 75% of the enzyme activity was maintained. However, enzyme activity was increased in the presence of AgNO3 and it was tolerant to solvents and detergents. Tannase II exhibited a better affinity for methyl gallate (Km = 1.42 mM) rather than for tannic acid (Km = 2.2 mM).
Conclusion: A. carbonarius tannase presented interesting properties as, for example, multi-tolerance, which highlight its potential for future application.

Aspergillus; Microbial enzymes; Solid-state fermentation; Tannase; Tannic acid

© Copyright 2015 - Electronic Journal of Biotechnology
Alternative site location:

Home Faq Resources Email Bioline
© Bioline International, 1989 - 2018, Site last up-dated on 09-Jul-2018.
Site created and maintained by the Reference Center on Environmental Information, CRIA, Brazil
System hosted by the Internet Data Center of Rede Nacional de Ensino e Pesquisa, RNP, Brazil