Heterologous expression of cellobiohydrolases in filamentous fungi: An update on the current challenges, achievements and perspectives

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Abstract

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.

Original languageEnglish
JournalProcess Biochemistry
Volume50
Issue number2
Pages (from-to)211-220
Number of pages10
ISSN1359-5113
DOIs
Publication statusPublished - Feb 2015

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Cellulose 1,4-beta-Cellobiosidase
Fungi
Enzymes
Cellulose
Biomass
Glycosylation
Trichoderma
Biofuels
Aspergillus
Post Translational Protein Processing
Protein Sorting Signals
Sugars
Hydrolysis
Polymers
Plasmids
Peptide Hydrolases
Crystalline materials
Proteins
Costs and Cost Analysis

Keywords

  • Cellobiohydrolase
  • Consolidated bioprocessing
  • Filamentous fungi
  • Heterologous expression
  • On-site enzyme production

Cite this

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title = "Heterologous expression of cellobiohydrolases in filamentous fungi: An update on the current challenges, achievements and perspectives",
abstract = "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.",
keywords = "Cellobiohydrolase, Consolidated bioprocessing, Filamentous fungi, Heterologous expression, On-site enzyme production, Cellobiohydrolase, Consolidated bioprocessing, Filamentous fungi, Heterologous expression, On-site enzyme production",
author = "Marta Zoglowek and L{\"u}beck, {Peter S.} and Ahring, {Birgitte K.} and Mette L{\"u}beck",
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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

VL - 50

SP - 211

EP - 220

JO - Process Biochemistry

JF - Process Biochemistry

SN - 1359-5113

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ER -