On the safety of Trichoderma reesei

Nevalainen, Helena; Suominen, Pirkko; Taimisto, Kaarina

doi:10.1016/0168-1656(94)90126-0

Cited by 98 publications

(52 citation statements)

References 38 publications

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“…However, although it was subsequently shown to be the anamorph of the pantropical ascomycete Hypocrea jecorina 2 , the organism remains most widely recognized by its former name. It has enjoyed a long history of safe use for industrial enzyme production 3 and as an important model system for studying lignocellulose degradation.…”

mentioning

confidence: 99%

“…Although genetic engineering techniques, gene knockout protocols and DNA-mediated transformation systems 3 have improved industrial enzyme-producing T. reesei strains, the need to better understand this fungus and expand its extraordinary biotechnological potential has given impetus to the quest to sequence its genome. To this end, we have now analyzed the T. reesei genome with particular emphasis on its potential contributions to fuel biotechnology and other industrial applications.…”

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confidence: 99%

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Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)

et al. 2008

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confidence: 99%

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confidence: 99%

Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)

et al. 2008

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“…A large number of mutant strains of T. reesei have been created worldwide by successive rounds of traditional mutagenesis and screening in an effort to obtain empirically higher-yielding strains which are capable of producing more efficient enzymes to satisfy industrial requirements (reviewed in [25]). However, such an economic imperative has introduced considerable confusion into the compilation of data pertaining to the structures and enzyme kinetics of Trichoderma cellulases across the plethora of T. reesei strains.…”

Section: Discussionmentioning

confidence: 99%

Modified glycosylation of cellobiohydrolase I from a high cellulase‐producing mutant strain of Trichoderma reesei

Harrison¹,

Nouwens²,

Jardine³

et al. 1998

European Journal of Biochemistry

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139

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Cellobiohydrolase I is an industrially important exocellulase secreted in high yields by the filamentous fungus Trichoderma reesei. The nature and effect of glycosylation of CBHI and other cellulolytic enzymes is largely unknown, although many other structural and mechanistic aspects of cellulolytic enzymes are well characterised. Using a combination of liquid chromatography, electrospray mass spectrometry, solidphase Edman degradation, and monosaccharide analysis we have identified every site of glycosylation of CBHI from a high cellulase-producing mutant strain of T. reesei, ALKO2877, and characterised each site in terms of its modifying carbohydrate and site-specific heterogeneity. The catalytic core domain comprises three N-linked glycans which each consist of a single N-acetylglucosamine residue. Within the glycopeptide linker domain, all eight threonines are variably glycosylated with between at least one, and up to three, mannose residues per site. All serines in this domain are at least partially glycosylated with a single mannose residue. This linker region has also been shown to be sulfated by a combination of ion chromatography and collision-induced dissociation electrospray mass spectrometry. The sulfate is probably mannose-linked. The biological significance of N-linked single N-acetylglucosamine in the catalytic core, and mannose sulfation in the linker region, is not known. Keywords : cellobiohydrolase I; cellulase; fungal glycosylation; Trichoderma; N-acetylglucosamine.Cellobiohydrolase I (CBHI) is the major family C glycoprotein secreted by the filamentous fungus Trichoderma reesei, where it operates in synergy with other exo-glucanases and endo-glucanases to achieve the degradation of cellulose [1]. CBHI is typically secreted in the order of several grams/litre, and many aspects of its structure and biology are well characterised. Like most other fungal cellulolytic enzymes characterised, CBHI conforms to a well-defined multi-domain structure, typified by a relatively large catalytic (core) domain spatially removed from a smaller cellulose-binding domain (CBD) by a highly O-glycosylated linker domain [2]. Presumably, the CBD serves as a form of anchor, and the linker a form of torsional leash, providing the catalytic region with access to a wide range of potential (and perhaps otherwise inaccessible) sites [3]. Although the catalytic domain of CBHI by itself is sufficient for cellulose binding and full catalytic activity at low enzyme to cellulose ratios, a functional CBD with sufficient spatial separation from the catalytic region is necessary for cellulolytic activity at higher enzyme-to-cellulose ratios [3]. The importance of the linker domain in maintaining spatial orientation of catalytic Correspondence to N. H. Packer,

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“…This biomass-degrading fungus represents a paradigm for the production of bioethanol and a range of key biochemical building blocks, such as aspartic acid, glucaric acid, glutamic acid, glycerol, sorbitol, and hydroxybutyrolactone, because it naturally possesses enzymes that hydrolyze lignocellulosic polysaccharides (Martinez et al, 2008;Alper & Stephanopoulos, 2009). It has enjoyed a long history of safe use in industrial enzyme production and is currently widely used as a source of cellulases and hemicellulases for the hydrolysis of plant cell wall polysaccharides (Nevalainen et al, 1994;Martinez et al, 2008). Although genetic engineering techniques, gene knockout protocols, and DNA-mediated transformation systems have improved the performance of industrial T. reesei strains (Martinez et al, 2008), further studies are needed to expand its extraordinary potential for biofuel production.…”

Section: Trichoderma Reeseimentioning

confidence: 99%

Innovative Biological Solutions to Challenges in Sustainable Biofuels Production

Yang¹,

Li²,

Weston³

et al. 2011

Biofuel Production-Recent Developments and Prospects

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On the safety of Trichoderma reesei

Cited by 98 publications

References 38 publications

Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)

Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)

Modified glycosylation of cellobiohydrolase I from a high cellulase‐producing mutant strain of Trichoderma reesei

Innovative Biological Solutions to Challenges in Sustainable Biofuels Production

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