Chrysoporthe cubensis: a new source of cellulases and hemicellulases to application in biomass saccharification processes.

نویسندگان

  • Daniel Luciano Falkoski
  • Valéria Monteze Guimarães
  • Maíra Nicolau de Almeida
  • Acelino Couto Alfenas
  • Jorge Luiz Colodette
  • Sebastião Tavares de Rezende
چکیده

The plant pathogenic fungus Chrysoporthe cubensis was cultivated under solid state employing different substrates and the highest endoglucanase (33.84Ug(-1)), FPase (2.52Ug(-1)), β-glucosidase (21.55Ug(-1)) and xylanase (362.38Ug(-1)) activities were obtained using wheat bran as carbon source. Cellulases and xylanase produced by C. cubensis showed maximal hydrolysis rate at pH 4.0 and in a temperature range of 50-60°C. All enzymatic activities were highly stable at 40 and 50°C through 48h of pre-incubation. Saccharification of alkaline pretreated sugarcane bagasse by crude enzyme extract from C. cubensis resulted in release of 320.8mg/g and 288.7mg/g of glucose and xylose, respectively. On another hand, a similar assay employing commercial cellulase preparation resulted in release of 250.6mg/g and 62.1mg/g of glucose and xylose, respectively. Cellulolytic extract from C. cubensis showed a great potential to be used in biomass saccharification processes.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Improved yield of α-L-arabinofuranosidase by newly isolated Aspergillus niger ADH-11 and synergistic effect of crude enzyme on saccharification of maize stover

Background: In the view of depleting resources and ever-increasing price of crude oil, there is an urge for the development of alternative sources to solve the issue of fuel in the coming years. Lignocellulosic biomass is considered to be the most potential alternative resources for fossil fuel. Bioconversion of cellulosic and hemicellulosic components into fermentable sugars is the key step in...

متن کامل

Novel hosts of the Eucalyptus canker pathogen Chrysoporthe cubensis and a new Chrysoporthe species from Colombia.

The pathogen Chrysoporthe cubensis (formerly Cryphonectria cubensis) is best known for the important canker disease that it causes on Eucalyptus species. This fungus is also a pathogen of Syzygium aromaticum (clove), which is native to Indonesia, and like Eucalyptus, is a member of Myrtaceae. Furthermore, C. cubensis has been found on Miconia spp. native to South America and residing in Melasto...

متن کامل

Structural and functional studies of the glycoside hydrolase family 3 β-glucosidase Cel3A from the moderately thermophilic fungus Rasamsonia emersonii

The filamentous fungus Hypocrea jecorina produces a number of cellulases and hemicellulases that act in a concerted fashion on biomass and degrade it into monomeric or oligomeric sugars. β-Glucosidases are involved in the last step of the degradation of cellulosic biomass and hydrolyse the β-glycosidic linkage between two adjacent molecules in dimers and oligomers of glucose. In this study, it ...

متن کامل

Lignin triggers irreversible cellulase loss during pretreated lignocellulosic biomass saccharification

BACKGROUND Non-productive binding of enzymes to lignin is thought to impede the saccharification efficiency of pretreated lignocellulosic biomass to fermentable sugars. Due to a lack of suitable analytical techniques that track binding of individual enzymes within complex protein mixtures and the difficulty in distinguishing the contribution of productive (binding to specific glycans) versus no...

متن کامل

Draft Genome Sequence of Talaromyces cellulolyticus Strain Y-94, a Source of Lignocellulosic Biomass-Degrading Enzymes

Talaromyces cellulolyticus (formerly Acremonium cellulolyticus) is a promising fungus for cellulase production. Here, we present the draft genome sequence of T. cellulolyticus strain Y-94. The genome is 36.4 Mbp long and contains genes for several enzymes involved in the degradation of lignocellulosic biomass, including cellulases, hemicellulases, pectinases, and amylases.

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Bioresource technology

دوره 130  شماره 

صفحات  -

تاریخ انتشار 2013