Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats

Tiwari, Rameshwar; Kumar, Kanika; Singh, Surender; Nain, Lata; Shukla, Pratyoosh

doi:10.3389/fmicb.2016.01597

Cited by 23 publications

(8 citation statements)

References 62 publications

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“…Among the three types of bacterial cellulases (EC 3.2.1.21) in glycoside hydrolase family of enzymes, β-glucosidases represent an important and ubiquitous class of hydrolases because they are capable of cleaving polysaccharides, the most abundant class of chemically identifiable compounds in the oceanic dissolved organic matter (DOM) pool, to available monosaccharide for consumption by biological organisms [ 26 , 27 , 28 ]. The diversity of β-glycosidase-producing bacteria has been studied in different habitats, including soil [ 29 ], cow dung and compost [ 30 ], and marine environments. The first study investigating the characteristics and diversity of β-glucosidase activity was reported in marine snow, where a β-glucosidase isoenzyme was detected by two different chromatographic separations and the same isoenzyme exhibited two peak of activity when eluted at lower NaCl concentrations [ 31 ].…”

Section: Introductionmentioning

confidence: 99%

High Diversity of β-Glucosidase-Producing Bacteria and Their Genes Associated with Scleractinian Corals

Xiao

et al. 2021

IJMS

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β-Glucosidase is a microbial cellulose multienzyme that plays an important role in the regulation of the entire cellulose hydrolysis process, which is the rate-limiting step in bacterial carbon cycling in marine environments. Despite its importance in coral reefs, the diversity of β-glucosidase-producing bacteria, their genes, and enzymatic characteristics are poorly understood. In this study, 87 β-glucosidase-producing cultivable bacteria were screened from 6 genera of corals. The isolates were assigned to 21 genera, distributed among three groups: Proteobacteria, Firmicutes, and Actinobacteria. In addition, metagenomics was used to explore the genetic diversity of bacterial β-glucosidase enzymes associated with scleractinian corals, which revealed that these enzymes mainly belong to the glycosidase hydrolase family 3 (GH3). Finally, a novel recombinant β-glucosidase, referred to as Mg9373, encompassing 670 amino acids and a molecular mass of 75.2 kDa, was classified as a member of the GH3 family and successfully expressed and characterized. Mg9373 exhibited excellent tolerance to ethanol, NaCl, and glucose. Collectively, these results suggest that the diversity of β-glucosidase-producing bacteria and genes associated with scleractinian corals is high and novel, indicating great potential for applications in the food industry and agriculture.

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Section: Introductionmentioning

confidence: 99%

High Diversity of β-Glucosidase-Producing Bacteria and Their Genes Associated with Scleractinian Corals

Xiao

et al. 2021

IJMS

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“…Therefore, in order to achieve high conversion efficiency for cellulose, understanding the β-glucosidase-producing microbial communities are significantly important. Several sets of degenerate primer have been designed to analyze βglucosidase genes diversity from different environmental niches [4][5][6][7][8][9]. β-glucosidases (β-D-glucoside glucohydrolase, EC 3.2.1.21) are ubiquitous enzymes found in archaea, eubacteria, to eukaryotes [10].…”

Section: Introductionmentioning

confidence: 99%

“…GH1 family show better glucose tolerance [21,22]. Comparative analysis of the 3D structures of GH1 β-glucosidases reveal the (β/α) 8 TIM-barrel architecture that is typical of this enzyme family [23]. De Giuseppe et al…”

Section: Introductionmentioning

confidence: 99%

β-glucosidase genes differentially expressed during composting

Zhang

Chen

et al. 2020

Preprint

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Background: Cellulose degradation by cellulase is brought about by complex communities of interacting microorganism, which significantly to the cycling of carbon on a global scale. β-Glucosidase is the rate-limiting enzyme of degradation of cellulose. Thus, analysis of expression of genes involved in cellulose degradation and regulation of β-glucosidase gene expression in composting is beneficial to a better understanding of cellulose degradation mechanism. According to our previous researches, we present the hypothesis that "microbial functional communities differentially regulate the expression of glucose-tolerant β-glucosidase and glucose sensitive βglucosidase (up or down regulation) to adapt to the changes in cellulose degradation."Results: Here, the functional microbial community structure and function change in association with cellulose degradation during the process of natural and inoculated composts was investigated by metatranscriptome and DNA clone library. Compared with inoculated compost, cellulose degradation was obviously inhibited during natural composting. Especially, the cooling phase of natural compost exhibited carbon catabolite repression (CCR) effect due to high concentration of glucose and cellobiose. The expression of genes encoding endoglucanase and exoglucanase were significantly down-regulation, while the CCR has no effect on β-glucosidase genes expression levels. But functional microbial community composition changed significantly, the composition of glucose-tolerant βglucosidase increased.Conclusions: These results indicated that microbial functional communities differentially regulate the expression of glucose tolerant β-glucosidase (up regulation) and non-glucose tolerant β-glucosidase (down regulation) under CCR. This work provides a frame work to predict how functional microbial communities will respond to cellulose degradation conditions changes.

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“…Substrates such as 4-nitrophenyl- β -D-galactopyranoside, 4-nitrophenyl- β -D-thioglucoside, and 4-nitrophenyl- β -D-glucopyranoside ( p NPG), are most commonly used artificial substrates in enzymatic assays for confirmation of β -glucosidase enzymes function ( Czjzek et al, 2000 ; Geerlings et al, 2000 ; Warzecha et al, 2000 ; Morant et al, 2008b ; Shaik et al, 2013 ; Tiwari et al, 2016 ). In order to examine functionality of Ce BGlu1 and Ce BGlu2, their hydrolytic activity against commercial substrate 4-nitrophenyl- β -D-glucopyranoside ( p NPG) was analyzed.…”

Section: Resultsmentioning

confidence: 99%

Functional Characterization of Genes Coding for Novel β-D-Glucosidases Involved in the Initial Step of Secoiridoid Glucosides Catabolism in Centaurium erythraea Rafn

et al. 2022

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Secoiridoid glucosides (SGs) are monoterpenoids derived from the iridoid cyclopentane-C-pyran skeleton with β-D glucose linked at C1 position. Coordinated metabolic processes, such as biosynthesis and catabolism of SGs, ensure constitutive presence of these bitter tasting compounds in plant tissues, which plays a decisive role in the defense against pathogens and herbivores. These compounds are susceptible to hydrolysis mediated by enzymes β-glucosidases, and the resulting aglycones are subsequently directed toward different metabolic pathways in plants. Function of two β-D-glucosidases (named CeBGlu1 and CeBGlu2) from centaury (Centaurium erythraea Rafn; fam. Gentianaceae), belonging to the glycoside hydrolase 1 (GH1) family, was confirmed using in vitro assays with recombinant proteins, following their heterologous expression in E. coli and His-tag affinity purification. Although they show slightly differential substrate preference, both isoforms display high specificity toward SGs and the organ-specific distribution of transcripts was positively correlated with the content of SGs in diploid and tetraploid C. erythraea plants. Transient overexpression of CeBGlu1 and CeBGlu2 in C. erythraea leaves induced changes in metabolite profiles. The effectiveness of transgene overexpression has been altered by plant ploidy. UHPLC/DAD/(±)HESI − MS2 profiling of leaves of diploid and tetraploid C. erythraea genotypes revealed that the amounts of major SGs; sweroside, swertiamarin, and gentiopicrin was decreased in agroinfiltrated leaves, especially when CeBGlu1 and CeBGlu2 were co-expressed with transgene silencing suppressor p19. The work demonstrates that in planta metabolic engineering adopting transient overexpression of CeBGlu1 and CeBGlu2 is a suitable tool for the modulation of SGs content and glucosides/aglycones ratio, which might have substantial effects on overall phytochemistry of C. erythraea.

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Molecular Detection and Environment-Specific Diversity of Glycosyl Hydrolase Family 1 β-Glucosidase in Different Habitats

Cited by 23 publications

References 62 publications

High Diversity of β-Glucosidase-Producing Bacteria and Their Genes Associated with Scleractinian Corals

High Diversity of β-Glucosidase-Producing Bacteria and Their Genes Associated with Scleractinian Corals

β-glucosidase genes differentially expressed during composting

Functional Characterization of Genes Coding for Novel β-D-Glucosidases Involved in the Initial Step of Secoiridoid Glucosides Catabolism in Centaurium erythraea Rafn

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