Characterization of acidic endoglucanase Cel12A from Gloeophyllum trabeum and its synergistic effects on hydrogen peroxide–acetic acid (HPAC)-pretreated lignocellulose

Oh, Chi Hoon; Park, Chan Song; Lee, Yoon Gyo; Song, Younho; Bae, Hyeun‐Jong

doi:10.1186/s10086-019-1803-7

Cited by 4 publications

(19 citation statements)

References 40 publications

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“…Rawat et al [ 50 ], instead, reported on a GH12 endo-glucanase from Aspergillus niger strongly inhibited by Cu 2+ , while the Zn 2+ inhibitory effect was only partial at the same concentration. The activity of a GH12 acidic endo-glucanase from Gloeophyllum trabeum was not affected by Zn 2+ and Cu 2+ , even at 50 mM concentrations [ 51 ]. Juturu and Wu [ 52 ] reviewed the effects of metals on xylanases belonging to different families (GH10, GH11 and GH39), all negatively affected by Hg +2 , Fe +2 , Co +2 , Mn +2 , Ag +2 , Pb +2 and Cu +2 , but they provided no clues about Zn 2+ and Ni 2+ .…”

Section: Resultsmentioning

confidence: 99%

Lupinus albus γ-Conglutin, a Protein Structurally Related to GH12 Xyloglucan-Specific Endo-Glucanase Inhibitor Proteins (XEGIPs), Shows Inhibitory Activity against GH2 β-Mannosidase

Benedetti

Galanti

Capraro

et al. 2020

IJMS

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γ-conglutin (γC) is a major protein of Lupinus albus seeds, but its function is still unknown. It shares high structural similarity with xyloglucan-specific endo-glucanase inhibitor proteins (XEGIPs) and, to a lesser extent, with Triticum aestivum endoxylanase inhibitors (TAXI-I), active against fungal glycoside hydrolases GH12 and GH11, respectively. However, γC lacks both these inhibitory activities. Since β-galactomannans are major components of the cell walls of endosperm in several legume plants, we tested the inhibitory activity of γC against a GH2 β-mannosidase (EC 3.2.1.25). γC was actually able to inhibit the enzyme, and this effect was enhanced by the presence of zinc ions. The stoichiometry of the γC/enzyme interaction was 1:1, and the calculated Ki was 1.55 μM. To obtain further insights into the interaction between γC and β-mannosidase, an in silico structural bioinformatic approach was followed, including some docking analyses. By and large, this work describes experimental findings that highlight new scenarios for understanding the natural role of γC. Although structural predictions can leave space for speculative interpretations, the full complexity of the data reported in this work allows one to hypothesize mechanisms of action for the basis of inhibition. At least two mechanisms seem plausible, both involving lupin-γC-peculiar structures.

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Section: Resultsmentioning

confidence: 99%

Lupinus albus γ-Conglutin, a Protein Structurally Related to GH12 Xyloglucan-Specific Endo-Glucanase Inhibitor Proteins (XEGIPs), Shows Inhibitory Activity against GH2 β-Mannosidase

Benedetti

Galanti

Capraro

et al. 2020

IJMS

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“…ER is an organelle in which several posttranslational modifications such as glycosylation or disulfide bond formation occur, thereby contributing to the functionality of produced proteins (Margolin et al, 2018(Margolin et al, , 2020a. Recently, Oh et al (2019) isolated and characterized the acidic endoglucanase GtCel12A (Gloeophyllum trabeum Cel12A). In this study, it was shown that this enzyme displayed highest activity on β-glucan, followed by lichenan and carboxymethyl cellulose (CMC) and xyloglucan (Miotto et al, 2014;Oh et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

“…In this study, it was shown that this enzyme displayed highest activity on β-glucan, followed by lichenan and carboxymethyl cellulose (CMC) and xyloglucan (Miotto et al, 2014;Oh et al, 2019). GtCel12A produced from Pichia pastoris displayed not only high enzymatic activity but also synergistic effects in combination with commercial cellulase on hydrogen peroxideacetic acid-pretreated lignocellulosic biomass (Oh et al, 2019). In this study, we attempted to produce GtCel12A from N. benthamiana to establish a plant-based platform for GtCel12A production.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Recently, Oh et al ( 2019 ) isolated and characterized the acidic endoglucanase GtCel12A ( Gloeophyllum trabeum Cel12A). In this study, it was shown that this enzyme displayed highest activity on β-glucan, followed by lichenan and carboxymethyl cellulose (CMC) and xyloglucan (Miotto et al, 2014 ; Oh et al, 2019 ). GtCel12A produced from Pichia pastoris displayed not only high enzymatic activity but also synergistic effects in combination with commercial cellulase on hydrogen peroxide-acetic acid-pretreated lignocellulosic biomass (Oh et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

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Production of Gloeophyllum trabeum Endoglucanase Cel12A in Nicotiana benthamiana for Cellulose Degradation

et al. 2021

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Lignocellulosic biomass from plants has been used as a biofuel source and the potent acidic endoglucanase GtCel12A has been isolated from Gloeophyllum trabeum, a filamentous fungus. In this study, we established a plant-based platform for the production of active GtCel12A fused to family 3 cellulose-binding module (CBM3). We used the signal sequence of binding immunoglobulin protein (BiP) and the endoplasmic reticulum (ER) retention signal for the accumulation of the produced GtCel12A in the ER. To achieve enhanced enzyme expression, we incorporated the M-domain of the human receptor-type tyrosine-protein phosphatase C into the construct. In addition, to enable the removal of N-terminal domains that are not necessary after protein expression, we further incorporated the cleavage site of Brachypodium distachyon small ubiquitin-like modifier. The GtCel12A-CBM3 fusion protein produced in the leaves of Nicotiana benthamiana exhibited not only high solubility but also efficient endoglucanase activity on the carboxymethyl cellulose substrate as determined by 3,5-dinitrosalicylic acid assay. The endoglucanase activity of GtCel12A-CBM3 was maintained even when immobilized on microcrystalline cellulose beads. Taken together, these results indicate that GtCel12A endoglucanase produced in plants might be used to provide monomeric sugars from lignocellulosic biomass for bioethanol production.

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Hydrolysis of ionic liquid–treated substrate with an Iocasia fonsfrigidae strain SP3-1 endoglucanase

Heng,

Sutheeworapong,

Wangnai

et al. 2024

Appl Microbiol Biotechnol

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Recently, we reported the discovery of a novel endoglucanase of the glycoside hydrolase family 12 (GH12), designated IfCelS12A, from the haloalkaliphilic anaerobic bacterium Iocasia fonsfrigidae strain SP3-1, which was isolated from a hypersaline pond in the Samut Sakhon province of Thailand (ca. 2017). IfCelS12A exhibits high substrate specificity on carboxymethyl cellulose and amorphous cellulose but low substrate specificity on b-1,3;1,4-glucan. Unlike some endoglucanases of the GH12 family, IfCelS12A does not exhibit hydrolytic activity on crystalline cellulose (i.e., Avicel™). High-Pressure Liquid Chromatography (HPLC) and Thin Layer Chromatography (TLC) analyses of products resulting from IfCelS12-mediated hydrolysis indicate mode of action for this enzyme. Notably, IfCelS12A preferentially hydrolyzes cellotetraoses, cellopentaoses, and cellohexaoses with negligible activity on cellobiose or cellotriose. Kinetic analysis with cellopentaose and barely b-d-glucan as cellulosic substrates were conducted. On cellopentaose, IfCelS12A demonstrates a 16-fold increase in activity (KM = 0.27 mM; kcat = 0.36 s−1; kcat/KM = 1.34 mM−1 s−1) compared to the enzymatic hydrolysis of barley b-d-glucan (KM: 0.04 mM, kcat: 0.51 s−1, kcat/KM = 0.08 mM−1 s−1). Moreover, IfCelS12A enzymatic efficacy is stable in hypersaline sodium chlorids (NaCl) solutions (up to 10% NaCl). Specifically, IfCel12A retains notable activity after 24 h at 2M NaCl (10% saline solution). IfCelS12A used as a cocktail component with other cellulolytic enzymes and in conjunction with mobile sequestration platform technology offers additional options for deconstruction of ionic liquid–pretreated cellulosic feedstock. Key points • IfCelS12A from an anaerobic alkaliphile Iocasia fronsfrigidae shows salt tolerance • IfCelS12A in cocktails with other enzymes efficiently degrades cellulosic biomass • IfCelS12A used with mobile enzyme sequestration platforms enhances hydrolysis

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Characterization of acidic endoglucanase Cel12A from Gloeophyllum trabeum and its synergistic effects on hydrogen peroxide–acetic acid (HPAC)-pretreated lignocellulose

Cited by 4 publications

References 40 publications

Lupinus albus γ-Conglutin, a Protein Structurally Related to GH12 Xyloglucan-Specific Endo-Glucanase Inhibitor Proteins (XEGIPs), Shows Inhibitory Activity against GH2 β-Mannosidase

Lupinus albus γ-Conglutin, a Protein Structurally Related to GH12 Xyloglucan-Specific Endo-Glucanase Inhibitor Proteins (XEGIPs), Shows Inhibitory Activity against GH2 β-Mannosidase

Production of Gloeophyllum trabeum Endoglucanase Cel12A in Nicotiana benthamiana for Cellulose Degradation

Hydrolysis of ionic liquid–treated substrate with an Iocasia fonsfrigidae strain SP3-1 endoglucanase

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