Lignocellulosic residues : Biodegradation and bioconversion by fungi

http://www.biotek.lu.se/fileadmin/bioteknik/Utbildning/Kurser/KKKA05/ProgressETOHprocess.pdf

Progress in bioethanol processing

Trends in bioconversion of lignocellulose: Biofuels, platform chemicals & biorefinery concept

Production of bioethanol from lignocellulosic materials via the biochemical pathway: a review.

In view of rising prices of crude oil due to increasing fuel demands, the need for alternative sources of bioenergy is expected to increase sharply in the coming years. Among potential alternative bioenergy resources, lignocellulosics have been identified as the prime source of biofuels and other value-added products. Lignocelluloses as agricultural, industrial and forest residuals account for the majority of the total biomass present in the world. To initiate the production of industrially important products from cellulosic biomass, bioconversion of the cellulosic components into fermentable sugars is necessary. A variety of microorganisms including bacteria and fungi may have the ability to degrade the cellulosic biomass to glucose monomers. Bacterial cellulases exist as discrete multi-enzyme complexes, called cellulosomes that consist of multiple subunits. Cellulolytic enzyme systems from the filamentous fungi, especially Trichoderma reesei, contain two exoglucanases or cellobiohydrolases (CBH1 and CBH2), at least four endoglucanases (EG1, EG2, EG3, EG5), and one β-glucosidase. These enzymes act synergistically to catalyse the hydrolysis of cellulose. Different physical parameters such as pH, temperature, adsorption, chemical factors like nitrogen, phosphorus, presence of phenolic compounds and other inhibitors can critically influence the bioconversion of lignocellulose. The production of cellulases by microbial cells is governed by genetic and biochemical controls including induction, catabolite repression, or end product inhibition. Several efforts have been made to increase the production of cellulases through strain improvement by mutagenesis. Various physical and chemical methods have been used to develop bacterial and fungal strains producing higher amounts of cellulase, all with limited success. Cellulosic bioconversion is a complex process and requires the synergistic action of the three enzymatic components consisting of endoglucanases, exoglucanases and β-glucosidases. The co-cultivation of microbes in fermentation can increase the quantity of the desirable components of the cellulase complex. An understanding of the molecular mechanism leading to biodegradation of lignocelluloses and the development of the bioprocessing potential of cellulolytic microorganisms might effectively be accomplished with recombinant DNA technology. For instance, cloning and sequencing of the various cellulolytic genes could economize the cellulase production process. Apart from that, metabolic engineering and genomics approaches have great potential for enhancing our understanding of the molecular mechanism of bioconversion of lignocelluloses to value added economically significant products in the future.

Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives

This review is written from the perspective of scientists working in lignocellulose bioconversion in a developing country and the aim of this review is to remind ourselves and other scientists working in related areas of lignocellulose research of the enormous economic potential of the bioprocessing of residual plant materials generally regarded as “waste”, and secondly to highlight some of the modern approaches which potentially could be used to tackle one of the major impediments, namely high enzyme cost, to speed-up the extensive commercialisation of the lignocellulose bioprocessing. Key words : lignocellulose, bioconversion, enzyme cost. 
African Journal of Biotechnology Vol. 2 (12), pp. 602-619, December 2003

/pdf/lignocellulose-biotechnology-issues-of-bioconversion-and-12x89zrkvn.pdf

Lignocellulose biotechnology: issues of bioconversion and enzyme production

The aim of this study was to purify and analyse a Phanerochaete chrysosporium cbh I.1 gene-product expressed as an inducible, secreted, heterologous protein from an Escerichia coli pGEX cbh I.1 clone. Using glutathione Sepharose 4B affinity chromatography, the expressed protein was purified from the supernatant of an induced E. coli transformed with pGEX cbh I.1 and ran as a single band on a Sodium dodecyl sulphate-polyacrylamide gel. The glutathione S-transferase (GST) fused CBHI.1 was approx-imately 80 kDa in size, approximately 2.2 kDa smaller than the theoretically predicted size. The purified protein exhibited time dependent hydrolytic reaction against carboxy-methyl-cellulose (CMC) and Avicel. On CMC the highest hydrolytic reaction occurred at 120 min. whereas for Avicel it was at 150 min. Optimum pH and temperature for activity of the protein against these cellulose substrates were pH 6 and 55oC, respectively, and the protein remained stable under these optimum conditions for 24 h. Key Words: Phanerochaete chrysosporium , cellobiohydrolase purification, heterologus expression. African Journal of Biotechnology Vol.3(7) 2004: 349-352

/pdf/characterisation-of-a-chimeric-phanerochaete-chrysosporium-2dqet94p3c.pdf

S Howard

Papers

Lignocellulose biotechnology: issues of bioconversion and enzyme production

Characterisation of a chimeric Phanerochaete chrysosporium cellobiohydrolase expressed from Escherichia coli