TY - JOUR
T1 - Heterologous expression of cellobiohydrolases in filamentous fungi
T2 - An update on the current challenges, achievements and perspectives
AU - Zoglowek, Marta
AU - Lübeck, Peter S.
AU - Ahring, Birgitte K.
AU - Lübeck, Mette
PY - 2015/2
Y1 - 2015/2
N2 - Cellobiohydrolases are among the most important enzymes functioning in the hydrolysis of crystalline cellulose, significantly contributing to the efficient biorefining of recalcitrant lignocellulosic biomass into biofuels and bio-based products. Filamentous fungi are recognized as both well-known producers of commercial preparations of cellulolytic enzymes and efficient hosts for heterologous protein secretion. Thus, Aspergillus and Trichoderma species have been chosen as hosts for the heterologous expression of native or engineered enzymes aiming at the overproduction of single enzymes or as hosts for the secretion of multi-enzyme cocktails for on-site production in biorefineries, which is important for reducing the costs of biomass conversion. An even more interesting aspect is consolidated bioprocessing, in which a single fungus both hydrolyzes lignocellulose polymers and ferments the resulting sugars into valuable products. However, due to low cellobiohydrolase activities, certain fungi might be deficient with regard to enzymes of value for cellulose conversion, and improving cellobiohydrolase expression in filamentous fungi has proven to be challenging. In this review, we examine the effects of altering promoters, signal peptides, culture conditions and host post-translational modifications. For heterologous cellobiohydrolase production in filamentous fungi to become an industrially feasible process, the construction of site-integrating plasmids, development of protease-deficient strains and glycosylation engineering are obvious targets for constructing efficient enzyme producers.
AB - Cellobiohydrolases are among the most important enzymes functioning in the hydrolysis of crystalline cellulose, significantly contributing to the efficient biorefining of recalcitrant lignocellulosic biomass into biofuels and bio-based products. Filamentous fungi are recognized as both well-known producers of commercial preparations of cellulolytic enzymes and efficient hosts for heterologous protein secretion. Thus, Aspergillus and Trichoderma species have been chosen as hosts for the heterologous expression of native or engineered enzymes aiming at the overproduction of single enzymes or as hosts for the secretion of multi-enzyme cocktails for on-site production in biorefineries, which is important for reducing the costs of biomass conversion. An even more interesting aspect is consolidated bioprocessing, in which a single fungus both hydrolyzes lignocellulose polymers and ferments the resulting sugars into valuable products. However, due to low cellobiohydrolase activities, certain fungi might be deficient with regard to enzymes of value for cellulose conversion, and improving cellobiohydrolase expression in filamentous fungi has proven to be challenging. In this review, we examine the effects of altering promoters, signal peptides, culture conditions and host post-translational modifications. For heterologous cellobiohydrolase production in filamentous fungi to become an industrially feasible process, the construction of site-integrating plasmids, development of protease-deficient strains and glycosylation engineering are obvious targets for constructing efficient enzyme producers.
KW - Cellobiohydrolase
KW - Consolidated bioprocessing
KW - Filamentous fungi
KW - Heterologous expression
KW - On-site enzyme production
KW - Cellobiohydrolase
KW - Consolidated bioprocessing
KW - Filamentous fungi
KW - Heterologous expression
KW - On-site enzyme production
U2 - 10.1016/j.procbio.2014.12.018
DO - 10.1016/j.procbio.2014.12.018
M3 - Review article
SN - 1359-5113
VL - 50
SP - 211
EP - 220
JO - Process Biochemistry
JF - Process Biochemistry
IS - 2
ER -