A Novel Application Potential of GH6 Cellobiohydrolase CtCel6 from Thermophilic Chaetomium thermophilum for Gene Cloning, Heterologous Expression and Biological Characterization

Zhou, Qinzheng; Jia, Jianchao; Ji, Peng; Han, Chao

doi:10.17957/ijab/15.0290

Cited by 11 publications

(3 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Most of the GH6 cellulases are optimally active in the acidic range such as Ctcel6 of Chaetomium thermophilum and TlCel6A of Talaromyces leycettanus (Zhou et al 2017 ; Gu et al 2019 ) and also GH7 CBHs of M. thermophila (MtCel7A) and C. thermophilum (CtCel7) (Kadowaki et al 2018 ; Han et al 2020 ). Only one CBH (MoCel6A) of Magnaporthe oryzae has been reported with the pH optima of 9.0 (Takahashi et al 2010 ).…”

Section: Discussionmentioning

confidence: 99%

Recombinant cellobiohydrolase of Myceliophthora thermophila: characterization and applicability in cellulose saccharification

2021

View full text Add to dashboard Cite

A codon optimized cellobiohydrolase (CBH) encoding synthetic gene of 1188 bp from a thermophilic mold Myceliophthora thermophila (MtCel6A) was cloned and heterologously expressed in Escherichia coli for the first time. In silico analysis suggested that MtCel6A is a GH6 CBH and belongs to CBHII family, which is structurally similar to Cel6A of Humicola insolens. The recombinant MtCel6A is expressed as active inclusion bodies, and the molecular mass of the purified enzyme is ~ 45 kDa. The rMtCel6A is active in a wide range of pH (4–12) and temperatures (40–100 °C) with optima at pH 10.0 and 60 °C. It exhibits T1/2 of 6.0 and 1.0 h at 60 and 90 °C, respectively. The rMtCel6A is an extremozyme with organic solvent, salt and alkali tolerance. The Km, Vmax, kcat and kcat/Km values of the enzyme are 3.2 mg mL−1, 222.2 μmol mg−1 min−1, 2492 s−1 and 778.7 s−1 mg−1 mL−1, respectively. The product analysis of rMtCel6A confirmed that it is an exoenzyme that acts from the non-reducing end of cellulose. The addition of rMtCel6A to the commercial cellulase mix (Cellic CTec2) led to 1.9-fold increase in saccharification of the pre-treated sugarcane bagasse. The rMtCel6A is a potential CBH that finds utility in industrial processes such as in bioethanol, paper pulp and textile industries. Graphical Abstract

show abstract

Section: Discussionmentioning

confidence: 99%

Recombinant cellobiohydrolase of Myceliophthora thermophila: characterization and applicability in cellulose saccharification

2021

View full text Add to dashboard Cite

show abstract

“…A GH6 cellulase from Chaetomium thermophilum was found to have maximal activity at pH 5 and 70°C (Zhou et al 2017). The broad specificity of PmGH is clearly due to its multi-modular structure.…”

Section: Discussionmentioning

confidence: 97%

Characterization and homology modelling of a novel multi-modular and multi-functional Paenibacillus mucilaginosus glycoside hydrolase

2019

View full text Add to dashboard Cite

Glycoside hydrolases, particularly cellulases, xylanases and mannanases, are essential for the depolymerisation of lignocellulosic substrates in various industrial bio-processes. In the present study, a novel glycoside hydrolase from Paenibacillus mucilaginosus (PmGH) was expressed in E. coli, purified and characterised. Functional analysis indicated that PmGH is a 130 kDa thermophilic multimodular and multi-functional enzyme, comprising a GH5, a GH6 and two CBM3 domains and exhibiting cellulase, mannanase and xylanase activities. The enzyme displayed optimum hydrolytic activities at pH 6 and 60°C and moderate thermostability. Homology modelling of the full-length protein highlighted the structural and functional novelty of native PmGH, with no close structural homologs identified. However, homology modelling of the individual GH5, GH6 and the two CBM3 domains yielded excellent models based on related structures from the Protein Data Bank. The catalytic GH5 and GH6 domains displayed a (β/α)8 and a distorted 7 stranded (β/α) fold, respectively. The distinct homology at the domain level but low homology of the full-length protein suggests that this protein evolved by exogenous gene acquisition and recombination.

show abstract

“…Among them, some are able to opportunistically cause systemic infections and trigger severe allergic reactions that increase the risk of developing asthma [ 7 ]. On the other hand, some species of the genus Chaetomium are plant endophytes [ 17 , 18 , 19 , 20 ], producing high levels of various enzymes [ 21 , 22 , 23 , 24 ], antioxidants [ 25 , 26 ], as well as antifungal [ 25 , 27 , 28 , 29 , 30 , 31 ], antibacterial [ 28 , 32 , 33 , 34 , 35 , 36 , 37 ], and nematicidal metabolites [ 38 , 39 ], possessing anticancer [ 26 , 28 , 30 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 ] and anti-inflammatory activities [ 39 , 52 ], and being able to biosynthesize several types of nanoparticles [ 44 , 53 , 54 ]. The genus includes psychrotolerant [ 55 ], mesophilic, thermotolerant, and thermophilic species [ 5 ], which are widely used in the medicin...…”

Section: Introductionmentioning

confidence: 99%

Chaetomium and Chaetomium-like Species from European Indoor Environments Include Dichotomopilus finlandicus sp. nov.

et al. 2021

View full text Add to dashboard Cite

The genus Chaetomium is a frequently occurring fungal taxon world-wide. Chaetomium and Chaetomium-like species occur in indoor environments, where they can degrade cellulose-based building materials, thereby causing structural damage. Furthermore, several species of this genus may also cause adverse effects on human health. The aims of this research were to identify Chaetomium and Chaetomium-like strains isolated from indoor environments in Hungary and Finland, two geographically distant regions of Europe with drier and wetter continental climates, respectively, and to study their morphological and physiological properties, as well as their extracellular enzyme activities, thereby comparing the Chaetomium and Chaetomium-like species isolated from these two different regions of Europe and their properties. Chaetomium and Chaetomium-like strains were isolated from flats and offices in Hungary, as well as from schools, flats, and offices in Finland. Fragments of the translation elongation factor 1α (tef1α), the second largest subunit of RNA polymerase II (rpb2) and β-tubulin (tub2) genes, as well as the internal transcribed spacer (ITS) region of the ribosomal RNA gene cluster were sequenced, and phylogenetic analysis of the sequences performed. Morphological examinations were performed by stereomicroscopy and scanning electron microscopy. Thirty-one Chaetomium sp. strains (15 from Hungary and 16 from Finland) were examined during the study. The most abundant species was Ch. globosum in both countries. In Hungary, 13 strains were identified as Ch. globosum, 1 as Ch. cochliodes, and 1 as Ch. interruptum. In Finland, 10 strains were Ch. globosum, 2 strains were Ch. cochliodes, 2 were Ch. rectangulare, and 2 isolates (SZMC 26527, SZMC 26529) proved to be representatives of a yet undescribed phylogenetic species from the closely related genus Dichotomopilus, which we formally describe here as the new species Dichotomopilus finlandicus. Growth of the isolates was examined at different temperatures (4, 15, 20, 25, 30, 37, 35, 40, and 45 °C), while their extracellular enzyme production was determined spectrophotometrically.

show abstract

A Novel Application Potential of GH6 Cellobiohydrolase CtCel6 from Thermophilic Chaetomium thermophilum for Gene Cloning, Heterologous Expression and Biological Characterization

Cited by 11 publications

References 31 publications

Recombinant cellobiohydrolase of Myceliophthora thermophila: characterization and applicability in cellulose saccharification

Recombinant cellobiohydrolase of Myceliophthora thermophila: characterization and applicability in cellulose saccharification

Characterization and homology modelling of a novel multi-modular and multi-functional Paenibacillus mucilaginosus glycoside hydrolase

Chaetomium and Chaetomium-like Species from European Indoor Environments Include Dichotomopilus finlandicus sp. nov.

Contact Info

Product

Resources

About