Purification and characterization of novel bi-functional GH3 family β-xylosidase/β-glucosidase from Aspergillus niger ADH-11

Patel, Harshvadan; Kumar, Adepu K.; Shah, Amita

doi:10.1016/j.ijbiomac.2017.11.132

Cited by 26 publications

(6 citation statements)

References 32 publications

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“…While it is common for glycosidases of the GH1 family to possess both β-glucosidase and β-galactosidase activity, β-xylosidase/xylanase activity is unusual for this family ( He and Withers, 1997 ). However, there are examples of other GH1 family hydrolases, which likewise show decent activity with the xylosidase substrate PNPX ( Liu et al, 2018 ; Yin et al, 2020 ) and promiscuous glycoside hydrolases of other GH families, mainly from the GH family 3, that show β-glucosidase as well as β-xylosidase activity, have also been reported ( Zhou et al, 2012 ; Gruninger et al, 2014 ; Patel et al, 2018 ).…”

Section: Discussionmentioning

confidence: 99%

Activity-Based Protein Profiling for the Identification of Novel Carbohydrate-Active Enzymes Involved in Xylan Degradation in the Hyperthermophilic Euryarchaeon Thermococcus sp. Strain 2319x1E

et al. 2022

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Activity-based protein profiling (ABPP) has so far scarcely been applied in Archaea in general and, especially, in extremophilic organisms. We herein isolated a novel Thermococcus strain designated sp. strain 2319x1E derived from the same enrichment culture as the recently reported Thermococcus sp. strain 2319x1. Both strains are able to grow with xylan as the sole carbon and energy source, and for Thermococcus sp. strain 2319x1E (optimal growth at 85°C, pH 6–7), the induction of xylanolytic activity in the presence of xylan was demonstrated. Since the solely sequence-based identification of xylanolytic enzymes is hardly possible, we established a complementary approach by conducting comparative full proteome analysis in combination with ABPP using α- or β-glycosidase selective probes and subsequent mass spectrometry (MS)-based analysis. This complementary proteomics approach in combination with recombinant protein expression and classical enzyme characterization enabled the identification of a novel bifunctional maltose-forming α-amylase and deacetylase (EGDIFPOO_00674) belonging to the GH57 family and a promiscuous β-glycosidase (EGIDFPOO_00532) with β-xylosidase activity. We thereby further substantiated the general applicability of ABPP in archaea and expanded the ABPP repertoire for the identification of glycoside hydrolases in hyperthermophiles.

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Section: Discussionmentioning

confidence: 99%

Activity-Based Protein Profiling for the Identification of Novel Carbohydrate-Active Enzymes Involved in Xylan Degradation in the Hyperthermophilic Euryarchaeon Thermococcus sp. Strain 2319x1E

et al. 2022

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“…Sequences were assembled in DNAStar (DNAStar, Inc., Madison, WI, USA) and trimmed on both ends to remove primer sequences. Alignment was carried out with the Muscle program ( 40 ) using MEGA X software ( 41 ), and the resulting alignment was subjected to DNA substitution model analysis to select the best-fitting model. Phylogenetic relationships were inferred using the Poisson correction model ( 42 ) and the neighbor-joining method.…”

Section: Methodsmentioning

confidence: 99%

“…Bootstrap support values were obtained from 1,000 random resamplings. Alignments were visualized using Jalview v2.11 ( 41 , 43 ), while trees were constructed using iTOL v5.2 as reported above.…”

Section: Methodsmentioning

confidence: 99%

Metabolomic and Transcriptional Profiling of Oleuropein Bioconversion into Hydroxytyrosol during Table Olive Fermentation by Lactiplantibacillus plantarum

Vaccalluzzo

Solieri

Tagliazucchi

et al. 2022

Appl Environ Microbiol

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The study aims to elucidate the mechanisms responsible for the bioconversion of oleuropein into low molecular weight phenolic compounds in two selected L. plantarum strains, namely C11C8 and F3.5, under stress brine conditions and at two different temperatures (16°C and 30°C). For this purpose, we adopted an experimental strategy that combined high-resolution mass spectrometry, in silico functional analysis of glycosidic hydrolases GH1 encoding candidate genes and gene expression study. Oleuropein hydrolysis products and underlying enzymatic steps were identified, as well as a novel putative bgl gene, using seven strains belonging to the same species as controls, was detected. According to metabolomic analysis, a new intermediate compound (decarboxymethyl dialdehydic form of oleuropein aglycone) was revealed. In addition, the strain C11C8 showed a decrease in oleuropein content higher than F3.5 strain (30% vs 15%) at the temperature of 16°C. The highest increase in hydroxytyrosol was depicted by the strain C11C8 at the temperature of 30°C. PCR assay and sequencing analysis revealed that both strains possess bglH_1 , bglH_2 and bglH3 genes. Furthermore, RT-PCR assay showed that bglH_3 is the only gene transcribed in all tested conditions, while bglH_2 is switched off in strain C11C8 grown under cold temperature and no transcription was detected for gene bglH_1 . BglH_3 gene encodes a 6-phospho-beta-glucosidase, suggesting how phospho-β-glucosidase activity could belong to the overall metabolic strategy undertaken by L. plantarum to survive in an environment poor in free sugars, like table olive. Importance In the present study, a new candidate gene bglH_3 responsible for the β-glucosidase positive phenotype in L. plantarum was detected, providing the basis for future marker-assisted selection of L. plantarum starter strains with β-glucosidase positive phenotype. Furthermore, the ability of selected strains to hydrolyse oleuropein at low temperature is important for application as starter culture on an industrial-scale.

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“…β-Xylosidase, a major component of hemicellulose degrading enzymes, is well known to degrade the non-reducing ends of β-1,4-linked D-xylose residues to release xylose and has been investigated in a variety of microorganisms, including bacteria, archaea, fungi, and plants [ 23 - 25 ]. In addition to the degradation of xylooligosaccharides, β-xylosidase has great potential in biotechnological applications, especially in the food, medicine, pulp, and paper industries [ 26 - 28 ].…”

Section: Introductionmentioning

confidence: 99%

Highly Efficient Biotransformation of Notoginsenoside R1 into Ginsenoside Rg1 by Dictyoglomus thermophilum β-xylosidase Xln-DT

Wang

Fang

et al. 2022

J. Microbiol. Biotechnol.

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Notoginsenoside R1 and ginsenoside Rg1 are the main active ingredients of Panax notoginseng, exhibiting anti-fatigue, anti-tumor, anti-inflammatory, and other activities. In a previous study, a GH39 β-xylosidase Xln-DT was responsible for the bioconversion of saponin, a natural active substance with a xylose group, with high selectivity for cleaving the outer xylose moiety of notoginsenoside R1 at the C-6 position, producing ginsenoside Rg1 with potent anti-fatigue activity. The optimal bioconversion temperature, pH, and enzyme dosage were obtained by optimizing the transformation conditions. Under optimal conditions (pH 6.0, 75 o C, enzyme dosage 1.0 U/ml), 1.0 g/l of notoginsenoside R1 was converted into 0.86 g/l of ginsenoside Rg1 within 30 min, with a molar conversion rate of approximately 100%. Furthermore, the in vivo anti-fatigue activity of notoginsenoside R1 and ginsenoside Rg1 were compared using a suitable rat model. Compared with the control group, the forced swimming time to exhaustion was prolonged in mice by 17.3% in the Rg1 high group (20 mg/kg•d). Additionally, the levels of hepatic glycogen (69.9-83.3% increase) and muscle glycogen (36.9-93.6% increase) were increased. In the Rg1 group, hemoglobin levels were also distinctly increased by treatment concentrations. Our findings indicate that treatment with ginsenoside Rg1 enhances the anti-fatigue effects. In this study, we reveal a GH39 βxylosidase displaying excellent hydrolytic activity to produce ginsenoside Rg1 in the pharmaceutical and food industries.

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Purification and characterization of novel bi-functional GH3 family β-xylosidase/β-glucosidase from Aspergillus niger ADH-11

Cited by 26 publications

References 32 publications

Activity-Based Protein Profiling for the Identification of Novel Carbohydrate-Active Enzymes Involved in Xylan Degradation in the Hyperthermophilic Euryarchaeon Thermococcus sp. Strain 2319x1E

Activity-Based Protein Profiling for the Identification of Novel Carbohydrate-Active Enzymes Involved in Xylan Degradation in the Hyperthermophilic Euryarchaeon Thermococcus sp. Strain 2319x1E

Metabolomic and Transcriptional Profiling of Oleuropein Bioconversion into Hydroxytyrosol during Table Olive Fermentation by Lactiplantibacillus plantarum

Highly Efficient Biotransformation of Notoginsenoside R1 into Ginsenoside Rg1 by Dictyoglomus thermophilum β-xylosidase Xln-DT

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