Xylanase and cellulase systems of Clostridium sp.: an insight on molecular approaches for strain improvement.

نویسندگان

  • Leya Thomas
  • Abhilash Joseph
  • Lalitha Devi Gottumukkala
چکیده

Bioethanol and biobutanol hold great promise as alternative biofuels, especially for transport sector, because they can be produced from lignocellulosic agro-industrial residues. From techno-economic point of view, the bioprocess for biofuels production should involve minimal processing steps. Consolidated bioprocessing (CBP), which combines various processing steps such as pretreatment, hydrolysis and fermentation in a single bioreactor, could be of great relevance for the production of bioethanol and biobutanol or solvents (acetone, butanol, ethanol), employing clostridia. For CBP, Clostridium holds best promise because it possesses multi-enzyme system involving cellulosome and xylanosome, which comprise several enzymes such as cellulases and xylanases. The aim of this article was to review the recent developments on enzyme systems of clostridia, especially xylanase and cellulase with an effort to analyse the information available on molecular approaches for the improvement of strains with ultimate aim to improve the efficiencies of hydrolysis and fermentation.

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

Characterization of Xylanase and Cellulase from Extremely Haloalkaliphilic Archaeon Natrinema Sp. Ssbjup-1 Isolated from Lonar Lake

The extremely halophilic archaeon Natrinema sp. strain SSBJUP-1, which produces extracellular cellulase and xylanase, was isolated from the Lonar Lake situated in Buldhana, Maharashtra. The enzymes were optimally active at pH 9–10 and temperature 40–60 C and they were most stable up to pH 11 and 16 % of NaCl concentration. The xylanase showed maximum activity at 50C and cellulase at 40C. Xylana...

متن کامل

Optimization of the Cellulase Free Xylanase Production by Immobilized Bacillus Pumilus

Background: The extracellular xylanase secreted by microorganisms is a hydrolytic enzyme, which arbitrarily cleaves the β-1, 4 backbone of the polysaccharide xylan; an enzyme used in the food processing, bio-pulping and bio-bleaching. The commercial production of the xylanase is limited because of a higher cost involvement, which can be overcome by the cost-effective production...

متن کامل

A cellulolytic and xylanolytic enzyme complex from an alkalothermoanaerobacterium, Tepidimicrobium xylanilyticum BT14.

A cellulolytic and xylanolytic enzyme complex-producing alkalothermoanaerobacterium strain, Tepidimicrobium xylanilyticum BT14 is described. The cell was Gram-positive, rod-shaped and endospore-forming. Based on 16S rRNA gene analysis and various lines of biochemical and physiological properties, the strain BT14 was a new member of the genus Tepidimicrobium. The strain BT14 cells had ability to...

متن کامل

Cellulose- and xylan-degrading thermophilic anaerobic bacteria from biocompost.

Nine thermophilic cellulolytic clostridial isolates and four other noncellulolytic bacterial isolates were isolated from self-heated biocompost via preliminary enrichment culture on microcrystalline cellulose. All cellulolytic isolates grew vigorously on cellulose, with the formation of either ethanol and acetate or acetate and formate as principal fermentation products as well as lactate and g...

متن کامل

Corrigendum: Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism

(a) BlCel5B in the crystallographic and closed configuration; (b) Bacillus halodurans Cel5B (BhCel5B) (PDB id: 4V2X) (c) Piromyces rhizinflata GH5 endoglucanase (PDB id: 3AYR); (d) Clostridium cellulolyticum GH5 endoglucanase (PDB id: 1EDG); (e) Clostridium cellulovorans GH5 endoglucanase (PDB id: 3NDY); (f) Bacteroides ovatus GH5 xyloglucanase (PDB id: 3ZMR); (g) Paenibacillus pabuli GH5 xylog...

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 158  شماره 

صفحات  -

تاریخ انتشار 2014