β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides

Rohman, Ali; Dijkstra, Bauke W.; Puspaningsih, Ni Nyoman Tri

doi:10.3390/ijms20225524

Cited by 57 publications

(33 citation statements)

References 158 publications

(233 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Existing β-xylosidases are associated with several limitations, such as poor efficiency, low thermostability, salt sensitivity, and by-product inhibition (Bao et al, 2012;Anand et al, 2013). Therefore, efforts have been made to discover novel candidates of β-xylosidases using metagenomic approaches, with which little success has been achieved (Wagschal et al, 2009;Jordan et al, 2016;Cheng et al, 2017;Sato et al, 2017;Liu et al, 2018;Rohman et al, 2019; Table 2). Of the available metagenomic β-xylosidases, fewer than 20 have been extensively characterized to date.…”

Section: Metagenomic β-Xylosidases and Their Characteristicsmentioning

confidence: 99%

“…Several β-xylosidases and metagenomic β-xylosidases have also been identified for their bifunctional enzymatic activities ( DeCastro et al, 2016 ; Rohman et al, 2019 ). Such β-xylosidases find applicability in bioethanol production along with the endo-xylanases for efficient release of sugars from the hemicellulose component of agro-residues ( Sae-Lee and Boonmee, 2014 ; Wang et al, 2015 ).…”

Section: Metagenomic β-Xylosidases and Their Characteristicsmentioning

confidence: 99%

See 1 more Smart Citation

Xylanolytic Extremozymes Retrieved From Environmental Metagenomes: Characteristics, Genetic Engineering, and Applications

Verma

Satyanarayana

2020

Front. Microbiol.

View full text Add to dashboard Cite

Xylanolytic enzymes have extensive applications in paper, food, and feed, pharmaceutical, and biofuel industries. These industries demand xylanases that are functional under extreme conditions, such as high temperature, acidic/alkaline pH, and others, which are prevailing in bioprocessing industries. Despite the availability of several xylan-hydrolyzing enzymes from cultured microbes, there is a huge gap between what is available and what industries require. DNA manipulations as well as protein-engineering techniques are also not quite satisfactory in generating xylanhydrolyzing extremozymes. With a compound annual growth rate of 6.6% of xylanhydrolyzing enzymes in the global market, there is a need for xylanolytic extremozymes. Therefore, metagenomic approaches have been employed to uncover hidden xylanolytic genes that were earlier inaccessible in culture-dependent approaches. Appreciable success has been achieved in retrieving several unusual xylanolytic enzymes with novel and desirable characteristics from different extreme environments using functional and sequence-based metagenomic approaches. Moreover, the Carbohydrate Active Enzymes database includes approximately 400 GH-10 and GH-11 unclassified xylanases. This review discusses sources, characteristics, and applications of xylanolytic enzymes obtained through metagenomic approaches and their amelioration by genetic engineering techniques.

show abstract

Section: Metagenomic β-Xylosidases and Their Characteristicsmentioning

confidence: 99%

Section: Metagenomic β-Xylosidases and Their Characteristicsmentioning

confidence: 99%

Xylanolytic Extremozymes Retrieved From Environmental Metagenomes: Characteristics, Genetic Engineering, and Applications

Verma

Satyanarayana

2020

Front. Microbiol.

View full text Add to dashboard Cite

show abstract

“…It is clear that X 3 is produced at the very first step of the reaction, while X 1 started to be accumulated after 60 min of reaction ( Figure S7). Accumulation of X 3 by a xylan GH11 degrading enzyme is a marker of a xylanase activity [56], just like X 1 is for GH43 [57]. This observation reflects the fact that enough small oligosaccharides have to be produced by the xylanase first before being hydrolysed by the xylosidase.…”

Section: Characterisation Of the Complexes On Plant Cell Wall Polysacmentioning

confidence: 95%

Characterisation of the Effect of the Spatial Organisation of Hemicellulases on the Hydrolysis of Plant Biomass Polymer

Enjalbert

Mare

Roblin

et al. 2020

IJMS

View full text Add to dashboard Cite

Synergism between enzymes is of crucial importance in cell metabolism. This synergism occurs often through a spatial organisation favouring proximity and substrate channelling. In this context, we developed a strategy for evaluating the impact of the geometry between two enzymes involved in nature in the recycling of the carbon derived from plant cell wall polymers. By using an innovative covalent association process using two protein fragments, Jo and In, we produced two bi-modular chimeric complexes connecting a xylanase and a xylosidase, involved in the deconstruction of xylose-based plant cell wall polymer. We first show that the intrinsic activity of the individual enzymes was preserved. Small Angle X-rays Scattering (SAXS) analysis of the complexes highlighted two different spatial organisations in solution, affecting both the distance between the enzymes (53 Å and 28 Å) and the distance between the catalytic pockets (94 Å and 75 Å). Reducing sugar and HPAEC-PAD analysis revealed different behaviour regarding the hydrolysis of Beechwood xylan. After 24 h of hydrolysis, one complex was able to release a higher amount of reducing sugar compare to the free enzymes (i.e., 15,640 and 14,549 µM of equivalent xylose, respectively). However, more interestingly, the two complexes were able to release variable percentages of xylooligosaccharides compared to the free enzymes. The structure of the complexes revealed some putative steric hindrance, which impacted both enzymatic efficiency and the product profile. This report shows that controlling the spatial geometry between two enzymes would help to better investigate synergism effect within complex multi-enzymatic machinery and control the final product.

show abstract

“…Merely, the thermostability of endo-1,4-β-xylanases from filamentous fungi can be improved by genetic engineering; thereby, the application scope of the filamentous fungi endo-1,4-β-xylanases is greatly extended (Li et al, 2019c ). All the β-xylosidases are mainly divided into GH1, GH3, GH30, GH39, GH43, GH52, GH54, and GH120 (Rohman et al, 2019 ). However, most β-xylosidases, especially the β-xylosidases belonging to GH3, are sensitive and inhibited to xylose by feedback, which limits its practical application.…”

Section: Introductionmentioning

confidence: 99%

Co-production of Xylooligosaccharides and Xylose From Poplar Sawdust by Recombinant Endo-1,4-β-Xylanase and β-Xylosidase Mixture Hydrolysis

Jiang

Tong

et al. 2021

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

As is well-known, endo-1,4-β-xylanase and β-xylosidase are the rate-limiting enzymes in the degradation of xylan (the major hemicellulosic component), main functions of which are cleavaging xylan to release xylooligosaccharides (XOS) and xylose that these two compounds have important application value in fuel, food, and other industries. This study focuses on enzymatic hydrolysis of poplar sawdust xylan for production of XOS and xylose by a GH11 endo-1,4-β-xylanase MxynB-8 and a GH39 β-xylosidase Xln-DT. MxynB-8 showed excellent ability to hydrolyze hemicellulose of broadleaf plants, such as poplar. Under optimized conditions (50°C, pH 6.0, dosage of 500 U/g, substrate concentration of 2 mg/mL), the final XOS yield was 85.5%, and the content of XOS2−3 reached 93.9% after 18 h. The enzymatic efficiency by MxynB-8 based on the poplar sawdust xylan in the raw material was 30.5%. Xln-DT showed excellent xylose/glucose/arabinose tolerance, which is applied as a candidate to apply in degradation of hemicellulose. In addition, the process and enzymatic mode of poplar sawdust xylan with MxynB-8 and Xln-DT were investigated. The results showed that the enzymatic hydrolysis yield of poplar sawdust xylan was improved by adding Xln-DT, and a xylose-rich hydrolysate could be obtained at high purity, with the xylose yield of 89.9%. The enzymatic hydrolysis yield was higher (32.2%) by using MxynB-8 and Xln-DT together. This study provides a deep understanding of double-enzyme synergetic enzymolysis of wood polysaccharides to valuable products.

show abstract

β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides

Cited by 57 publications

References 158 publications

Xylanolytic Extremozymes Retrieved From Environmental Metagenomes: Characteristics, Genetic Engineering, and Applications

Xylanolytic Extremozymes Retrieved From Environmental Metagenomes: Characteristics, Genetic Engineering, and Applications

Characterisation of the Effect of the Spatial Organisation of Hemicellulases on the Hydrolysis of Plant Biomass Polymer

Co-production of Xylooligosaccharides and Xylose From Poplar Sawdust by Recombinant Endo-1,4-β-Xylanase and β-Xylosidase Mixture Hydrolysis

Contact Info

Product

Resources

About