Endogenous cellulolytic enzyme systems in the longhorn beetle &amp;lt;italic&amp;gt;Mesosa myops&amp;lt;/italic&amp;gt; (Insecta: Coleoptera) studied by transcriptomic analysis

Liu, Jie; Song, Ke-Qing; Teng, Huajing; Zhang, Bin; Li, Wenzhu; Xue, Huai‐Jun; Yang, Xingke

doi:10.1093/abbs/gmv070

Cited by 21 publications

(15 citation statements)

References 37 publications

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“…GH1 enzymes have broad catalytic and substrate specificities and function as β-xylosidases, β-glucuronidases, β-galactosidases, β-mannosidases or exo-β-1,4-glucanases, serving to hydrolyse substrates released from the hemicellulose matrix. CAZymes include > 40 GH45 cellulases and 4230 records of GH5, including the activities of enzymes like β-mannosidase (EC 3.2.1.25), chitosanase (EC 3.2.1.132), endo-β-1,4-glucanase (endocellulase, EC 3.2.1.4) and others [ 79 ]. Several Lamiinae longhorn beetles contain relatively large numbers of copies of GH5 cellulase [ 80 , 81 ].…”

Section: Discussionmentioning

confidence: 99%

De novo transcriptome assembly of the bamboo snout beetle Cyrtotrachelus buqueti reveals ability to degrade lignocellulose of bamboo feedstock

Luo

Liao

et al. 2018

Biotechnol Biofuels

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BackgroundThe bamboo weevil Cyrtotrachelus buqueti, which is considered a pest species, damages bamboo shoots via its piercing–sucking mode of feeding. C. buqueti is well known for its ability to transform bamboo shoot biomass into nutrients and energy for growth, development and reproduction with high specificity and efficacy of bioconversion. Woody bamboo is a perennial grass that is a potential feedstock for lignocellulosic biomass because of its high growth rate and lignocellulose content. To verify our hypothesis that C. buqueti efficiently degrades bamboo lignocellulose, we assessed the bamboo lignocellulose-degrading ability of this insect through RNA sequencing for identifying a potential route for utilisation of bamboo biomass.ResultsAnalysis of carbohydrate-active enzyme (CAZyme) family genes in the developmental transcriptome of C. buqueti revealed 1082 unigenes, including 55 glycoside hydrolases (GH) families containing 309 GHs, 51 glycosyltransferases (GT) families containing 329 GTs, 8 carbohydrate esterases (CE) families containing 174 CEs, 6 polysaccharide lyases (PL) families containing 11 PLs, 8 auxiliary activities (AA) families containing 131 enzymes with AAs and 17 carbohydrate-binding modules (CBM) families containing 128 CBMs. We used weighted gene co-expression network analysis to analyse developmental RNA sequencing data, and 19 unique modules were identified in the analysis. Of these modules, the expression of MEyellow module genes was unique and the module included numerous CAZyme family genes. CAZyme genes in this module were divided into two groups depending on whether gene expression was higher in the adult/larval stages or in the egg/pupal stages. Enzyme assays revealed that cellulase activity was highest in the midgut whereas lignin-degrading enzyme activity was highest in the hindgut, consistent with findings from intestinal gene expression studies. We also analysed the expression of CAZyme genes in the transcriptome of C. buqueti from two cities and found that several genes were also assigned to CAZyme families. The insect had genes and enzymes associated with lignocellulose degradation, the expression of which differed with developmental stage and intestinal region.ConclusionCyrtotrachelus buqueti exhibits lignocellulose degradation-related enzymes and genes, most notably CAZyme family genes. CAZyme family genes showed differences in expression at different developmental stages, with adults being more effective at cellulose degradation and larvae at lignin degradation, as well as at different regions of the intestine, with the midgut being more cellulolytic than the hindgut. This degradative system could be utilised for the bioconversion of bamboo lignocellulosic biomass.Electronic supplementary materialThe online version of this article (10.1186/s13068-018-1291-9) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

De novo transcriptome assembly of the bamboo snout beetle Cyrtotrachelus buqueti reveals ability to degrade lignocellulose of bamboo feedstock

Luo

Liao

et al. 2018

Biotechnol Biofuels

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“…It is suggested that MaCel1 may be a new member of the insect cellulase gene and its catalytic properties should be further investigated. There are different types of cellulase in different types of insects [43]. The β-D-Glucosidase activity of the MaCel1 was higher than that of the M. alternatus digestive tract previously reported, which might be caused by the different test objects [25].…”

Section: Discussionmentioning

confidence: 94%

Molecular Cloning and Expression Analysis of the Endogenous Cellulase Gene MaCel1 in Monochamus alternatus

Chen

Chu

et al. 2020

Forests

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The purpose of this study was to characterize the endogenous cellulase gene MaCel1 of Monochamus alternatus, which is an important vector of Bursaphelenchus xylophilus, a pine wood nematode, which causes pine wilt disease (PWD). In this study, MaCel1 was cloned by rapid amplification of cDNA end (RACE), and its expression analyzed by RT-qPCR (real-time quantitative PCR detecting). A total of 1778 bp of cDNA was obtained. The encoding region of this gene was 1509 bp in length, encoding a protein containing 502 amino acids with a molecular weight of 58.66 kDa, and the isoelectric point of 5.46. Sequence similarity analysis showed that the amino acids sequence of MaCel1 had high similarity with the β-Glucosinolate of Anoplophoraglabripennis and slightly lower similarity with other insect cellulase genes (GH1). The β-D-Glucosidase activity of MaCel1 was 256.02 ± 43.14 U/L with no β-Glucosinolate activity. MaCel1 gene was widely expressed in the intestine of M. alternatus. The expression level of MaCel1 gene in male (3.46) and female (3.51) adults was significantly higher than that in other developmental stages, and the lowest was in pupal stage (0.15). The results will help reveal the digestive mechanism of M. alternatus and lay the foundation for controlling PWD by controlling M. alternatus.

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“…Two proteins were assigned to GH45, which exhibits endoglucanase activity [16]. The CAZymes include more than 40 GH45 cellulases, including the activities of different enzymes, such as β-mannosidase (EC 3.2.1.25), chitosanase (EC 3.2.1.132), endo-β-1,4-glucanase (endocellulase, EC 3.2.1.4) and others [20]. Eleven candidates were assigned to GH5, which exhibits endoglucanase activity [21].…”

Section: Resultsmentioning

confidence: 99%

Degradation of bamboo lignocellulose by bamboo snout beetle Cyrtotrachelus buqueti in vivo and vitro: efficiency and mechanism

Luo

Chen

et al. 2019

Biotechnol Biofuels

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Background As an important biomass raw material, the lignocellulose in bamboo is of significant value in energy conversion. The conversion of bamboo lignocellulose into fermentable reducing sugar, i.e. the degradation of bamboo lignocellulose, is an important step in lignocellulose conversion. However, little research has focussed on excavating the enzymes and microbes that are related to the degradation of bamboo lignocellulose, which is important for its utilisation. This study used Cyrtotrachelus buqueti (bamboo snout beetle) to evaluate the efficiency of bamboo lignocellulose degradation. Results RNA sequencing was conducted to sequence the transcriptome of the insect before and after feeding on bamboo shoots. The expression levels of genes encoding several carbohydrate-active enzymes, such as endoglucanase ( evgtrinloc27093t1 and evgtrinloc16407t0 ) and laccase ( evgtrinloc15173t0 and evgtrinloc11252t0 ), were found to be upregulated after feeding. Faecal component analysis showed that the degradation efficiencies of cellulose, hemicellulose and lignin were 61.82%, 87.65% and 69.05%, respectively. After 6 days of co-culture with crude enzymes in vitro, the degradation efficiencies of cellulose, hemicellulose and lignin in bamboo shoot particles (BSPs) were 24.98%, 37.52% and 26.67%, respectively. These results indicated that lignocellulosic enzymes and related enzymes within the insect itself co-degraded bamboo lignocellulose. These finding can potentially be used for the pre-treatment and enzymatic hydrolysis of bamboo lignocellulose. Conclusion Our results showed that intestinal digestive enzymes from C. buqueti degraded bamboo shoot lignocellulose both in vivo and in vitro. In addition, the expression levels of many carbohydrate-active enzyme (CAZyme) genes were upregulated in the transcriptome, including those for cellulase, xylanase and ligninase genes. Therefore, we proposed a scheme for applying the lignocellulolytic enzymes from C. buqueti to degrade bamboo lignocellulose using genetic, enzymatic and fermentation engineering techniques to overexpress the lignocellulolytic enzymes genes in vitro and obtain large quantities of enzymes that could efficiently degrade bamboo lignocellulose and be used for lignocellulose bioconversion. Electronic supplementary material The online version of this article (10.1186/s13068-019-1406-y) contains supplementary material, which is available to authorized users.

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Endogenous cellulolytic enzyme systems in the longhorn beetle <italic>Mesosa myops</italic> (Insecta: Coleoptera) studied by transcriptomic analysis

Cited by 21 publications

References 37 publications

De novo transcriptome assembly of the bamboo snout beetle Cyrtotrachelus buqueti reveals ability to degrade lignocellulose of bamboo feedstock

De novo transcriptome assembly of the bamboo snout beetle Cyrtotrachelus buqueti reveals ability to degrade lignocellulose of bamboo feedstock

Molecular Cloning and Expression Analysis of the Endogenous Cellulase Gene MaCel1 in Monochamus alternatus

Degradation of bamboo lignocellulose by bamboo snout beetle Cyrtotrachelus buqueti in vivo and vitro: efficiency and mechanism

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