Heterologous expression and characterization of a xylanase and xylosidase from white rot fungi and their application in synergistic hydrolysis of lignocellulose

Zhuo, Rui; Yu, Hongbo; Qin, Xing; Ni, Haoxiang; Zhen, Jiang; Ma, Fuying; Zhang, Xiaoyu

doi:10.1016/j.chemosphere.2018.08.062

Cited by 38 publications

(14 citation statements)

References 38 publications

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“…The three xylanases could maintain relative activities of greater than 80% in the presence of Zn 2+ , Mg 2+ , Co 2+ and Ni 2+ . In contrast, the xylanases Xyl-IIb from P. citrinum HZN13 [30] and rXyn162 from Pleurotus ostreatus HAUCC 162 [31] retained relative activities of only 18% and 56% in the presence of 10 mM Ni 2+ , respectively. In addition, the xylanases xyn10B [20] and XYN11A [32] from P. oxalicum GZ-2 retained relative activities of only 37.2% and 67.8% in the presence of 10 mM Co 2+ , respectively.…”

Section: Resultsmentioning

confidence: 99%

Cooperation of hydrolysis modes among xylanases reveals the mechanism of hemicellulose hydrolysis by Penicillium chrysogenum P33

Yang

Wang

et al. 2019

Microb Cell Fact

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Background Xylanases randomly cleave the internal β-1,4-glycosidic bonds in the xylan backbone and are grouped into different families in the carbohydrate-active enzyme (CAZy) database. Although multiple xylanases are detected in single strains of many filamentous fungi, no study has been reported on the composition, synergistic effect, and mode of action in a complete set of xylanases secreted by the same microorganism. Results All three xylanases secreted by Penicillium chrysogenum P33 were expressed and characterized. The enzymes Xyl1 and Xyl3 belong to the GH10 family and Xyl3 contains a CBM1 domain at its C-terminal, whereas Xyl2 belongs to the GH11 family. The optimal temperature/pH values were 35 °C/6.0, 50 °C/5.0 and 55 °C/6.0 for Xyl1, Xyl2, and Xyl3, respectively. The three xylanases exhibited synergistic effects, with the maximum synergy observed between Xyl3 and Xyl2, which are from different families. The synergy between xylanases could also improve the hydrolysis of cellulase (C), with the maximum amount of reducing sugars (5.68 mg/mL) observed using the combination of C + Xyl2 + Xyl3. Although the enzymatic activity of Xyl1 toward xylan was low, it was shown to be capable of hydrolyzing xylooligosaccharides into xylose. Xyl2 was shown to hydrolyze xylan to long-chain xylooligosaccharides, whereas Xyl3 hydrolyzed xylan to xylooligosaccharides with a lower degree of polymerization. Conclusions Synergistic effect exists among different xylanases, and it was higher between xylanases from different families. The cooperation of hydrolysis modes comprised the primary mechanism for the observed synergy between different xylanases. This study demonstrated, for the first time, that the hydrolysates of GH11 xylanases can be further hydrolyzed by GH10 xylanases, but not vice versa.

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Section: Resultsmentioning

confidence: 99%

Cooperation of hydrolysis modes among xylanases reveals the mechanism of hemicellulose hydrolysis by Penicillium chrysogenum P33

Yang

Wang

et al. 2019

Microb Cell Fact

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“…In another research, two different sources of xylanase (rXyn162 and rXylCD2) exhibited synergistic hydrolysis of oat spelts xylan and sodium hydroxide pretreated corn stover (SHPC). These xylanase could efficiently improve the hydrolysis of SHPC by commercial cellulase [29]. Moreover, Ming-Hsu Chen et al discussed the synergistic effect of cellulase and xylanase from the SEM of material structure and composition analysis, and the result show that the synergistic effect could reduce the amount of cellulase added in the saccharification process [30].…”

Section: Discussionmentioning

confidence: 99%

Co-expression of cellulase and xylanase genes in Saccharomyces cerevisiae toward enhanced bioethanol production from corn stover

Xiao

Xia

et al. 2019

Bioengineered

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Lignocellulose is considered as a good resource for producing renewable energy. Previous in vitro studies have shown the synergistic action between cellulase and xylanase during lignocellulose biohydrolysis. In order to achieve the same effect in S. cerevisiae to enhance the practical biotransformation, two recombinant Saccharomyces cerevisiae strains (INVSc1-CBH-CA and INVSc1-CBH-TS) with co-expressed cellulase and xylanase were constructed. The cellulase and xylanase activities in INVSc1-CBH-CA and INVSc1-CBH-TS were 716.43 U/mL and 205.13 U/mL, 931.27 U/mL and 413.70 U/ mL, respectively. The recombinant S. cerevisiae can use the partly delignified corn stover (PDCS) more efficiently and more ethanol producted than S. cerevisiae only expressing cellulase. Fermentation with INVSc1-CBH-CA and INVSc1-CBH-TS using PDCS ethanol yields increased by 1.7 and 2.1 folds higher than INVSc1-CBH, 2.8 and 3.4 folds higher than the wild type S. cerevisiae. The strategy of co-expression cellulase and xylanase in saccharomyces cerevisiae is effective and can be a foundation to research the mechanism of synergy effect of cellulose and xylanase.

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“…Cornstalk and corn bran pretreatments were performed according to Zhuo et al [5]. The milled cornstalk and corn bran samples were autoclaved at 120 °C for 1 h with 1% (w/v) sodium hydroxide at a 10% ratio (w/v).…”

Section: Methodsmentioning

confidence: 99%

“…Because hemicellulose is concatenated with cellulose via hydrogen bonds and is chemically cross-linked with lignin, it is naturally resistant to digestion by cellulases. Thus, hemicellulose degradation can help cellulases access cellulose, resulting in more efficient cellulose utilization [4, 5]. Therefore, a more efficient means of enzymatic hemicellulose depolymerization in the biofuel and biorefinery industries is desired.…”

Section: Introductionmentioning

confidence: 99%

A GH51 α-l-arabinofuranosidase from Talaromyces leycettanus strain JCM12802 that selectively drives synergistic lignocellulose hydrolysis

Meng

et al. 2019

Microb Cell Fact

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Background The development of sustainable technologies for plant cell wall degradation greatly depends on enzymes with hydrolytic activities against carbohydrates. The waste by-products of agricultural cereals are important biomass sources because they contain large amounts of saccharides. Achieving efficient debranching and depolymerization are two important objectives for increasing the utilization of such renewable bioresources. GH51 α- l -arabinofuranosidases are important in biomass pretreatment because they act synergistically with other enzymes during hemicellulose hydrolysis. Results A GH51 α- l -arabinofuranosidase from Talaromyces leycettanus JCM12802 was heterologously expressed in Pichia pastoris GS115 and characterized. The recombinant α- l -arabinofuranosidase, Tl Abf51, showed an optimum temperature and pH of 55–60 °C and 3.5–4.0, respectively, and remained stable at 50 °C and pH 3.0–9.0. Tl Abf51 showed a higher catalytic efficiency (5712 mM −1 s −1 ) than most fungal α- l -arabinofuranosidases towards the substrate 4-nitrophenyl-α- l -arabinofuranoside. Moreover, Tl Abf51 preferentially removed 1,2- or 1,3-linked arabinofuranose residues from arabinoxylan and acted synergistically with the bifunctional xylanase/cellulase Tc Xyn10A at an activity ratio of 5:1. The highest yields of arabinose and xylooligosaccharides were obtained when Tl Abf51 was added after Tc Xyn10A or when both enzymes were added simultaneously. High-performance anion-exchange chromatography analyses showed that (i) arabinose and xylooligosaccharides with low degrees of polymerization (DP1–DP5) and (ii) arabinose and xylooligosaccharides (DP1–DP3) were the major hydrolysates obtained during the hydrolysis of sodium hydroxide-pretreated cornstalk and corn bran, respectively. Conclusions In contrast to other fungal GH51 α- l -arabinofuranosidases, recombinant Tl Abf51 showed excellent stability over a broad pH range and high catalytic efficiency. Moreover, Tl Abf51 acted synergistically with another hemicellulase to digest arabino-polysaccharides. These favorable enzymatic properties make Tl Abf51 attractive for biomass pretreatment and biofuel production. Electronic supplementary material The online version of this article (10.1186/s12934-019-1192-z) contains supplementary material, which is available to authorized users.

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Heterologous expression and characterization of a xylanase and xylosidase from white rot fungi and their application in synergistic hydrolysis of lignocellulose

Cited by 38 publications

References 38 publications

Cooperation of hydrolysis modes among xylanases reveals the mechanism of hemicellulose hydrolysis by Penicillium chrysogenum P33

Cooperation of hydrolysis modes among xylanases reveals the mechanism of hemicellulose hydrolysis by Penicillium chrysogenum P33

Co-expression of cellulase and xylanase genes in Saccharomyces cerevisiae toward enhanced bioethanol production from corn stover

A GH51 α-l-arabinofuranosidase from Talaromyces leycettanus strain JCM12802 that selectively drives synergistic lignocellulose hydrolysis

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