End-to-end gene fusions and their impact on the production of multifunctional biomass degrading enzymes.
The reduction of fossil fuels, coupled with its increase in price, has made the search for alternative energy resources more plausible. One of the topics gaining fast interest is the utilization of lignocellulose, the main component of plants. Its primary constituents, cellulose and hemicellulose, can be degraded by a series of enzymes present in microorganisms, into simple sugars, later used for bioethanol production. Thermophilic bacteria have proven to be an interesting source of enzymes required for hydrolysis since they can withstand high and denaturing temperatures, which are usually required for processes involving biomass degradation. However, the cost associated with the whole enzymatic process is staggering. A solution for cost effective and highly active production is through the construction of multifunctional enzyme complexes harboring the function of more than one enzyme needed for the hydrolysis process. There are various strategies for the degradation of complex biomass ranging from the regulation of the enzymes involved, to cellulosomes, and proteins harboring more than one enzymatic activity. In this review, the construction of multifunctional biomass degrading enzymes through end-to-end gene fusions, and its impact on production and activity by choosing the enzymes and linkers is assessed.
Institute of Technical Microbiology, Hamburg University of Technology (TUHH), Kasernenstr. 12, D-21073 Hamburg, Germany. mazen.rizk@tuhh.de
Mazen
M
Rizk
Garabed
G
Antranikian
Skander
S
Elleuche
D019677:Artificial Gene Fusion / Q000379:methods*; D055162:Biocatalysis; D001711:Biotransformation; D002482:Cellulose / Q000737:chemistry / Q000378:metabolism*; D004798:Enzymes / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D006868:Hydrolysis; D008031:Lignin / Q000737:chemistry / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D014990:Xylans / Q000737:chemistry / Q000378:metabolism*
D004798:Enzymes; D011993:Recombinant Fusion Proteins; D014990:Xylans; D002482:Cellulose; D008031:Lignin