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Glycoside Hydrolases

Glycoside hydrolases are a diverse group of enzymens that catalyze the hydrolysis of glycosidic bonds in carbohydrates.
These versatile enzymes play crucial roles in various biological processes, including biomass deconstruction, cell wall remodeling, and glycan metabolism.
Glycoside hydrolases are widely studied for their potential applications in biofuel production, food processing, and therapeutic interventions.
Researchers can leverage PubCompare.ai to efficiently identify the most accurate and reproducible protocols from the literature, preprints, and patents, optimizing their glycoside hydrolase studies and enhancing research efficiency and accuracy.

Most cited protocols related to «Glycoside Hydrolases»

1
Rumen Microbiome Profiling and Metabolic Reconstruction
Cited 14 times
One winter rumen fluid sample was separated into a pellet of plant material (gentle centrifugation for 5 mins at 3000 g) and the supernatant was sequentially filtered through a 0.8 μm filter and then onto a 0.2 μm filter. DNA was extracted from four fractions: the pellet (1 g), half of the biomass retained on each of the 0.8 and 0.2 μm filters, and the filtrate that passed through the 0.2 μm filter. DNA was sequenced with Illumina Hi-Seq 2500 (Columbus, OH, USA) at The Ohio State University. 16S rRNA gene sequences were reconstructed from the Illumina trimmed unassembled reads using EMIRGE (Miller et al., 2011 (link)). Trimmed reads were assembled de novo to generate genome fragments using IDBA-UD (Peng et al., 2012 (link)). Genes were called, annotated and analyzed as previously described by Wrighton et al. (2012) (link) (see Supplementary Methods for details). A combination of phylogenetic signal, coverage and GC content was used to identify BS11 genomic bins (Sharon et al., 2013 (link)). Additional assembly and binning methods and validation information are available in the Supplementary Methods. Genomic completion of the BS11 bins was assessed based on the presence of a core gene set that typically occurs only once per genome and is widely conserved among bacteria and archaea (Wu and Eisen, 2008 (link)). For sequence-based comparison, average amino acid identity (AAI) and average nucleotide identity (ANI) values were calculated using the ANI and AAI calculators from the Kostas lab calculator (http://enve-omics.ce.gatech.edu/).
Existing reference datasets for the 11 ribosomal proteins chosen as single-copy phylogenetic marker genes (RpL2, 3, 4, 6, 14, 15, 16 and 18, and RpS8, 17 and 19) were augmented with sequences mined from sequenced genomes from the Bacteroidales phyla from the NCBI and JGI IMG databases (August 2015). Each individual protein dataset was aligned using MUSCLE 3.8.31 and then manually curated to remove end gaps (Edgar, 2004 (link)). Alignments were concatenated to form an 11-gene, 63 taxa alignment and then run through ProtPipeliner, a python script developed in-house for generation of phylogenetic trees (https://github.com/lmsolden/protpipeliner). The pipeline runs as follows: alignments are curated with minimal editing by GBLOCKS (Talavara and Castresana, 2007 (link)), and model selection conducted via ProtTest 3.4 (Darriba et al., 2011 (link)). A maximum likelihood phylogeny for the concatenated alignment was conducted using RAxML version 8.3.1 under the LG model of evolution with 100 bootstrap replicates (Stamatakis, 2014 (link)) and visualized in iTOL (Letunic and Bork, 2007 (link)). Identified glycoside hydrolases of selected functional classes (for example, chitin, hemicellulose and debranching) were identified by a Pfam HMM search. Briefly, Pfam search was performed and parsed into an output table organized by function per genome. In addition, we manually identified genes for central carbonmetabolism, motility and fermentation product generation in all genomes.
Solden L.M., Hoyt D.W., Collins W.B., Plank J.E., Daly R.A., Hildebrand E., Beavers T.J., Wolfe R., Nicora C.D., Purvine S.O., Carstensen M., Lipton M.S., Spalinger D.E., Firkins J.L., Wolfe B.A, & Wrighton K.C. (2016). New roles in hemicellulosic sugar fermentation for the uncultivated Bacteroidetes family BS11. The ISME Journal, 11(3), 691-703.
Publication 2016
Amino Acids Archaea Bacteria Biological Evolution Centrifugation Chitin Fermentation Genes Genetic Markers Genome Glycoside Hydrolases hemicellulose Iron Motility, Cell Muscle Tissue Nucleotides Plants Proteins Python Ribosomal Proteins RNA, Ribosomal, 16S Rumen
2
Metagenomic Analysis of Glycoside Hydrolases
Cited 9 times
Genomic DNA extracted from the day 31 sample was used for sequencing library construction following the DOE Joint Genome Institute standard operating procedure for shotgun sequencing using the Roche 454 GS FLX Titanium technology. Obtained sequencing reads were quality trimmed and assembled using the Newbler assembler software (version 2) by 454 Life Sciences. For assembly, minimum acceptable overlap match (mi) was set to 0.95. Quality filtered sequence reads and assembled contigs ≥100 bp totaling 110 Mbp were used for further analysis. For global functional analysis, the metagenomic data set was loaded into MG-RAST [37] (link) and compared to other annotated metagenomes that are publicly available in the metagenome analysis platform. Correspondence analysis was performed using the R software package ade4 [38] .
Glycoside hydrolases of selected functional classes (e.g. cellulases, endohemicellulases, debranching enzymes) were identified using pfam HMMs (Pfam version 23.0 and HMMER v2.3). For the 3 GH families 44, 51 and 74 that are not represented in pfam, HMMs were generated (two for each, since they are 2-domain proteins) and treated similar to the pfam HMMs. For GH families covered by multiple pfams (e.g. GH2 or GH42) only the best scoring hit was taken into account in case there were multiple hits to the same contig. Contig read depth was factored as following: based on the Newbler output, the number of reads in each was determined and multiplied by the median read length of 400 bp and divided by the contig length. This weighting corrects approximately for differences in species abundance distribution (i.e. dominant populations producing higher depth contigs will be weighted in the analysis).
To extract potential full-length glycoside hydrolases from the metagenome data, we ran BLASTX on all contigs ≥1 kb against the CAZy [3] (link) and FOLy [39] (link) databases (E<1e−10), and filtered out hits matching the target enzyme over at least 90% of its length, and for which the target enzyme has a known enzymatic function (EC number listed in CAZy or FOLy). Frameshifts (most likely introduced by homopolymers during sequencing) were delineated by BLASTX of the targeted contigs against the non-redundant NCBI nucleotide database and corrected by deleting or duplicating single bases so as to maximize the BLAST scores. After manual frameshift correction, genes were called using fgenesb (http://www.softberry.com). For phylogenetic analysis, peptide sequences of the two full-length GH9 enzymes were aligned to reference sequences using ClustalX [40] (link) and imported into the ARB software package [41] (link) for phylogenetic reconstructions using the PROML function of the integrated Phylip package.
Allgaier M., Reddy A., Park J.I., Ivanova N., D'haeseleer P., Lowry S., Sapra R., Hazen T.C., Simmons B.A., VanderGheynst J.S, & Hugenholtz P. (2010). Targeted Discovery of Glycoside Hydrolases from a Switchgrass-Adapted Compost Community. PLoS ONE, 5(1), e8812.
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Publication 2010
BP 400 Cellulases DNA Library Enzymes Frameshift Mutation Genes Genome Glycoside Hydrolases Hypertelorism, Severe, With Midface Prominence, Myopia, Mental Retardation, And Bone Fragility Joints Metagenome Nucleotides Peptides Population Group Proteins Radioallergosorbent Test Titanium
3
Rabbit and Macaque Immunization with HIV Env Proteins
Cited 8 times
The BG505 SOSIP.664 trimers, gp120 monomers and WT.SEKS uncleaved gp140 proteins were all produced and purified as reported previously (9 (link), 13 (link), 19 (link)). Unless specified, the proteins were expressed in HEK293T cells by transient transfection and purified via a 2G12 MAb-affinity column followed by size-exclusion chromatography (SEC). Protein purities and properties were comparable to those described elsewhere (9 (link), 13 (link), 19 (link)). BG505 SOSIP.664 trimers were also expressed in HEK293S cells that lack N-acetylglucosaminyltransferase I (GnTI−/−). The resulting Env proteins bear glycans that are not fully processed and remain in oligomannose form (21 (link), 22 (link)). Samples of the 293S cell-derived trimers were treated with the EndoH glycosidase, as previously described, to reduce their total glycan content (22 (link)). The clade B B41 SOSIP.664 and B41 SOSIP.664-D7324 trimers were produced from stable CHO cell lines that were cultured in 0.5% serum (23 (link)). The trimers were purified by 2G12 affinity chromatography followed by SEC, as described elsewhere; the extent of V3-clipping was negligible (23 (link)). The YU2 gp140-Fd protein was made in HEK293T cells under contract for IAVI by Dr. Guillaume Stewart-Jones (University of Oxford, Oxford, UK), as described elsewhere (44 (link)).
Rabbit immunizations and blood sampling were carried out under subcontract at Covance (Denver, PA) according to the schedule presented in fig. S1B. Female New Zealand White rabbits (usually 4 per group) were immunized intramuscularly with 30 µg of the various Env proteins (40 µg in experiment 3). The proteins were formulated in 75 Units of ISCOMATRIX™, a saponin-based adjuvant obtained from CSL Ltd. (Parkville, Victoria, Australia) (45 (link)). Macaque immunizations and blood sampling were carried out at the Wisconsin Primate Center according to the schedule in fig. S1B. Rhesus macaques (4 per group) were immunized intramuscularly with 100 µg of BG505 SOSIP.664 or gp120 proteins formulated in 75 Units of ISCOMATRIX™.
Sanders R.W., van Gils M.J., Derking R., Sok D., Ketas T.J., Burger J.A., Ozorowski G., Cupo A., Simonich C., Goo L., Arendt H., Kim H.J., Lee J.H., Pugach P., Williams M., Debnath G., Moldt B., van Breemen M.J., Isik G., Medina-Ramírez M., Back J.W., Koff W., Julien J.P., Rakasz E.G., Seaman M.S., Guttman M., Lee K.K., Klasse P.J., LaBranche C., Schief W.R., Wilson I.A., Overbaugh J., Burton D.R., Ward A.B., Montefiori D.C., Dean H, & Moore J.P. (2015). HIV Neutralizing Antibodies Induced by Native-like Envelope Trimers. Science (New York, N.Y.), 349(6244), aac4223.
Publication 2015
alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I Bears Cell Lines Cells CHO Cells Chromatography, Affinity Females Gel Chromatography Gene Products, env Glycoside Hydrolases GP 140 HIV Envelope Protein gp120 Immunization ISCOMATRIX Macaca Macaca mulatta New Zealand Rabbits Pharmaceutical Adjuvants Polysaccharides Primates Proteins Rabbits Saponin Serum Transfection Transients
4
Revealing N-Glycan Profiles in Mouse Brain Tissue
Cited 7 times
Sectioned mouse brain tissue samples were mounted on ITO coated slides, and desiccated at room temperature for 20 minutes. A sequential ethanol wash was done in 70% ethanol for two minutes, two times, and one wash in 100% ethanol for two minutes, then a final desiccation at room temperature for 10 minutes. An ImagePrep spray station (Bruker Daltonics) was used to coat the slide with a 0.2 ml solution containing 20 ul of 1 mg/ml PNGaseF stock in water. This solution was sprayed by the ImagePrep using settings originally optimized for spraying of trypsin that result in minimal volumes and retention of spatial distribution8 (link),20 (link). If sialidase was used, 0.1 units of enzyme were diluted in 200uL water and sprayed following PNGaseF application using the same ImagePrep settings. Control tissue slices were blocked with a glass slide during the spraying process. Following application of glycosidase, slides were then incubated at 37°C for 2 hrs in a humidified chamber, then dried in a desiccator prior to matrix application. 2,5-Dihydroxybenzoic acid (DHB) matrix at a concentration of 0.2M in 50%MeOH 1%TFA was sprayed on to the slide using the ImagePrep for positive ion mode analysis. Spectra were acquired across the entire tissue section on a Solarix 70 dual source 7T FTICR mass spectrometer (Bruker Daltonics) to detect the N-glycans (m/z = 690–5000) with a SmartBeam II laser operating at 1000 Hz, a laser spot size of 25 µm and a raster width of 125µm unless otherwise indicated. For each laser spot, 1000 spectra were averaged. Images of differentially expressed glycans were generated to view the expression pattern of each analyte of interest using FlexImaging 3.0 software (Bruker Daltonics). Following MS analysis, data was loaded into FlexImaging Software focusing on the range m/z = 1200–4500 and reduced to 0.98 ICR Reduction Noise Threshold. Glycans were identified by selecting peaks that appeared in an average mass spectrum from the tissue that received PNGaseF application but did not appear in the control tissue. Observed glycans were searched against the glycan database provided by the Consortium for Functional Glycomics24 and known glycans that exist in mouse brain.
Powers T.W., Jones E.E., Betesh L.R., Romano P., Gao P., Copland J.A., Mehta A.S, & Drake R.R. (2013). A MALDI Imaging Mass Spectrometry Workflow for Spatial Profiling Analysis of N-linked Glycan Expression in Tissues. Analytical chemistry, 85(20), 9799-9806.
Publication 2013
2,3-dihydroxybenzoic acid Brain Enzymes Ethanol Glycoside Hydrolases Mass Spectrometry Mice, Laboratory Neuraminidase Polysaccharides Retention (Psychology) Tissues Trypsin
5
Comparative Genomics of Microbotryum Fungus
Cited 6 times
We compared M. lychnidis-dioicae to 18 other fungi (Additional file 13) that sample the three subphyla in Basidiomycota, including 5 other Pucciniomycotina, 7 Agaricomycotina, 3 Ustilaginomycotina, as well as 3 Ascomycota outgroups. For M. lychnidis-dioicae and the 18 other fungal genomes, we identified ortholog clusters using OrthoMCL [126 (link)] version 1.4 with a Markov inflation index of 1.5 and a maximum e-value of 1 × 10−5. Two genomes, R. glutinis and P. placenta, are missing more broadly conserved orthologs than the other genomes; examining the 961 Microbotryum gene clusters with an ortholog missing in just one other genome, the number of missing clusters in any one Basidiomycete genome ranged from 1 to 34 with the exception of R. glutinis and P. placenta, missing 410 and 393 of these highly conserved clusters, respectively. PFAM domains within each gene were identified using Hmmer3 [127 (link)], and gene ontology terms were assigned using BLAST2GO [128 (link)].
To examine gene duplication history, the phylome, or complete collection of phylogenetic trees for each gene in a genome, was reconstructed for Microbotryum lychnidis-dioicae and 19 other fungi, including those used for OrthoMCL (Additional file 13) and Serpula lacrymans. Phylomes were reconstructed using the previously described pipeline [129 (link)]. All trees and alignments have been deposited in PhylomeDB [129 (link)] and can be browsed on-line (www.phylomedb.org, phylome code 180). Trees were scanned to detect and date duplication events [130 ].
RNAi components from other other fungi were used as Blast queries to find homologs in M. lychnidis-dioicae; the queries used include U. hordei RdRp (CCF48827.1), C. neoformans Ago1 (XP_003194007), and N. crassa Dcl2 (Q75CC1.3) and Dcl1 (Q758J7.1). The putative function was confirmed by examining protein domains. The identified domains for each protein include: Piwi, PAZ and DUF1785 found in both copies of Argonaute (MVLG_06823, MVLG_06899); DEAD/DEAH helicase, double-stranded RNA binding, and RNAseIII (MVLG_01202). Sugar transporters were identified based on homology to the Ustillago maydis Srt1t transporter (Genbank: XP_758521) and the Uromyces viciae-fabae Hxt1 (Genbank: CAC41332).
The M. lychnidis-dioicae protein models corresponding to carbohydrate-active enzymes were assigned to families of glycoside hydrolases (GH), polysaccharide lyases (PL), carbohydrate esterases (CE), carbohydrate-binding modules (CBM), auxiliary activities (AA) and glycosyltransferases (GT) listed by the CAZy database [64 (link)], exactly as previously done for the analyses of dozens of fungal genomes [39 (link), 66 (link), 131 (link), 132 (link)].
Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J., Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E., Badouin H., Andrews J., Razeeq D., Gabaldón T., Quesneville H., Giraud T., Hood M.E., Schultz D.J, & Cuomo C.A. (2015). Sex and parasites: genomic and transcriptomic analysis of Microbotryum lychnidis-dioicae, the biotrophic and plant-castrating anther smut fungus. BMC Genomics, 16(1), 461.
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Publication 2015
Argonaute Proteins Ascomycetes Basidiomycota Carbohydrate Binding Modules Carbohydrates Cryptococcus neoformans DNA Helicases Enzymes Esterases Fungi Gene Duplication Genes Genome Genome, Fungal Glycoside Hydrolases Glycosyltransferase Membrane Transport Proteins Microbotryum lychnidis-dioicae M protein, multiple myeloma Placenta Polysaccharide-Lyases Protein Domain Rhodotorula glutinis RNA, Double-Stranded RNA Interference Serpula lacrymans Trees Uromyces viciae-fabae

Most recents protocols related to «Glycoside Hydrolases»

1
Deglycosylation of Purified ACE Protein
An ACE de-glycosylation kit (abcam) was used to de-glycosylate purified ACE protein according to the manufacturer’s instructions. A total of 30 μg of ACE protein was mixed with PNGase F, O-glycosidase, or α-2(3, 6, 8, 9)-neuraminidase to remove N-glycosylation, O-glycosylation, or sialic acid. De-glycosylated ACE was analyzed by Western botting, and its activity was examined.
Gao Y., Sun Y., Islam S., Nakamura T., Tomita T., Zou K, & Michikawa M. (2023). Presenilin 1 deficiency impairs Aβ42-to-Aβ40- and angiotensin-converting activities of ACE. Frontiers in Aging Neuroscience, 15, 1098034.
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Publication 2023
Glycopeptidase F Glycoside Hydrolases N-Acetylneuraminic Acid Neuraminidase protein S, human Staphylococcal Protein A
2
Glycoside Hydrolase Substrate Specificity
In order to analyze the hydrolysis substrate specificity of the DogH glycoside hydrolase, nine carbohydrates with different glycosidic bonds were selected for analysis in this study, as listed in Table 2. According to [17 (link)], the method of Benedict’s experiment was used to detect the reducing sugar content of the hydrolyzed substrates. Benedict’s experiment was conducted for a range of concentrations of glucose and maltose to confirm the differences between mono- and disaccharides and to determine reasonable concentrations for the main analysis; the standard curves are shown in Supplementary Figure S6. The final concentrations of reducing and non-reducing sugars were 0.25% and 0.5%, respectively. Amylase decomposition of starch was used as a positive control. Moreover, 200 μg/mL of DogH and an equivalent buffer solution without DogH were added to the solution and incubated at 37 °C for 4 h. The reaction was subsequently terminated by the addition of 500 μL of Benedict’s experiment and incubated at 95 °C for 10 min. The absorbance value of each sample was measured at 320 nm to determine the extent of copper reduction in the substrate. Three replicates of each carbohydrate were measured in the presence and absence of DogH addition.
Gui Y., Lin M., Yan Y., Jiang S., Zhou Z, & Wang J. (2023). A Novel Glycoside Hydrolase DogH Utilizing Soluble Starch to Maltose Improve Osmotic Tolerance in Deinococcus radiodurans. International Journal of Molecular Sciences, 24(4), 3437.
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Publication 2023
Amylase Buffers Carbohydrates Cardiac Glycosides Copper Disaccharides Exhaling Glucose Glycoside Hydrolases Hydrolysis Maltose Starch Sugars
3
Bioinformatic Analysis of DogH Proteins
Using the SignalP 5.0 software [57 (link)], we performed an analysis of DogH sequence signal peptides in D. radiodurans R1 strains and searched for homologous GH10 structural domains according to the UniProt database. The GH10 sequence was downloaded from the UniProt database and the glycoside hydrolase database CAZy, and the DogH sequence similarity was assessed using the BLASTp algorithm, while multiple sequence alignment was performed in MEGA 7.0 [58 (link)]. Sequences that did not contain conserved catalytic residues were removed from the alignment and the neighbor joining method was applied [59 (link)]. The results of the CLUSTAL X alignment were used to construct a phylogenetic tree using the MEGA 7.0 software. Two sets of evolutionary trees containing 33 sequences of glycoside hydrolase and 30 sequences of DogH protein were selected for analysis. We used SWISS-MODEL [60 (link)] to construct structural models based on the closest PDB homologs (crystal: 5oq2.1.A, Cwp19 protein [17 (link)]) and visualized the predicted structure in Adobe Photoshop. We then used the SWISS-MODEL server to identify and align putative homologs of the GHL10 domain (residues 62 to 339) of unknown function.
Gui Y., Lin M., Yan Y., Jiang S., Zhou Z, & Wang J. (2023). A Novel Glycoside Hydrolase DogH Utilizing Soluble Starch to Maltose Improve Osmotic Tolerance in Deinococcus radiodurans. International Journal of Molecular Sciences, 24(4), 3437.
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Publication 2023
Amino Acid Sequence Biological Evolution Catalysis Glycoside Hydrolases Proteins Sequence Alignment Sequence Analysis, Protein Strains Trees
4
Comprehensive Honey Phytochemical and Enzymatic Analysis
The total phenolic compounds, flavonoids and antioxidant capacity (DPPH and FRAP methods) were determined according to the methodology previously described by Tomczyk et al. (2021) [61 (link)]. For the analysis, 20% solutions of honey in distilled water were used.
The protein content in honey was determined using the Bradford method according to Latimer (2016) [62 ]. Briefly, 1 mL of Bradford reagent (Biorad, Hercules, CA, USA) was added to 100 μL of each honey solution (20% in distilled water). Samples were incubated for 5 min at ambient temperature and the absorbance was read at 595 nm using a spectrophotometer (Biomate 3, Thermo Scientific, Waltham, MA, USA). The results were calculated on the basis of a calibration curve (y = 31.752x, r2 = 0.9919) prepared for bovine serum albumin in the range of 6.25–200 µg.
Diastase number was determined by spectrophotometric method with the Phadebas Honey Diastase test (Magle AB, Lund, Sweden) strictly according to the manufacturer′s instructions. The values of the diastase number (DN) were calculated using the following Equation (1):
The activity of three glycosidases: N-acetyl-β-glucosaminidase (NAG), β-galactosidase (β-GAL) and acid phosphatase (AP) was determined in tested honey samples according to the procedure described by Sidor et al. (2021) [44 (link)], using appropriate p-nitrophenolic substrate. The absorbance of released p-nitrophenol was measured using microplate reader (EPOCH2, BioTek, Winooski, VT, USA) at λ = 400 nm. Results were expressed as enzymatic units U (µmol/min/g).
Tomczyk M., Czerniecka-Kubicka A., Miłek M., Sidor E, & Dżugan M. (2023). Tracking of Thermal, Physicochemical, and Biological Parameters of a Long-Term Stored Honey Artificially Adulterated with Sugar Syrups. Molecules, 28(4), 1736.
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Publication 2023
Acid Phosphatase Amylase Antioxidants beta-Galactosidase Enzymes Flavonoids Glucosaminidases Glycoside Hydrolases Honey Nitrophenols Proteins Serum Albumin, Bovine Spectrophotometry
5
Enzymatic Profiling of Yeast Strains
The enzymatic activity of the yeast strains was determined using the API ZYM test (BioMerieux, Lyon, France) in accordance with the manufacturer’s instructions. This test is a semiquantitative method that detects 19 enzymes, including proteases, glycosidases, lipases, and phosphatases. The concentrations of the yeast suspensions were adjusted with a standard 0.5 McFarland barium sulfate solution, which simulates a concentration of 1 × 106 CFU mL−1 of yeast approximately [50 (link),51 (link)]. After 48 h of culture in YPD broth, yeasts were recovered from the culture medium by centrifugation (10,000× g for 5 min), resuspended in sterile PBS, and adjusted to an optical density of 5 McFarland. Then, 65 µL of this suspension was deposited in the 20 wells of each gallery. The galleries were placed in an incubation chamber and incubated at 37 °C for 5 h. Enzyme activity was recorded as positive (+), medium (±), or negative (−) according to the color intensity of each reaction compared with an API-ZYM color reaction chart [36 (link)]. Medium and positive enzyme activity levels were considered positive.
Reinoso S., Gutiérrez M.S., Domínguez-Borbor C., Argüello-Guevara W., Bohórquez-Cruz M., Sonnenholzner S., Nova-Baza D., Mardones C, & Navarrete P. (2023). Selection of Autochthonous Yeasts Isolated from the Intestinal Tracts of Cobia Fish (Rachycentron canadum) with Probiotic Potential. Journal of Fungi, 9(2), 274.
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Publication 2023
Centrifugation enzyme activity Enzymes Glycoside Hydrolases Lipase Peptide Hydrolases Phosphoric Monoester Hydrolases Simulate composite resin Sterility, Reproductive Strains Sulfate, Barium Test, Clinical Enzyme Yeast, Dried Yeasts

Top products related to «Glycoside Hydrolases»

1
Pngase f by New England Biolabs
Sourced in United States, United Kingdom, Germany, Japan, Canada, France, China, Morocco, Italy
PNGase F is an enzyme that cleaves the bond between the asparagine residue and the N-acetylglucosamine residue in N-linked glycoproteins. It is commonly used in the analysis and characterization of glycoproteins.
2
O glycosidase by New England Biolabs
Sourced in United States, Japan
O-glycosidase is an enzyme that catalyzes the removal of O-linked glycosidic bonds from glycoproteins. It is used in biochemical research and analysis for the study of protein glycosylation patterns.
3
Endo h by New England Biolabs
Sourced in United States, United Kingdom, Germany, Canada, Switzerland, France
Endo H is a glycosidase enzyme that cleaves the chitobiose core of high mannose and some hybrid-type oligosaccharides from N-linked glycoproteins. It removes the N-linked glycans from glycoproteins, allowing the study of the effects of glycosylation on protein structure and function.
4
N glycosidase f by Roche
Sourced in United States, Germany
N-glycosidase F is a recombinant enzyme that cleaves the bond between the asparagine residue and the first N-acetylglucosamine residue of N-linked glycoproteins. It is used to remove N-linked glycans from glycoproteins for analysis and characterization.
5
Neuraminidase by New England Biolabs
Sourced in United States
Neuraminidase is an enzyme that catalyzes the removal of terminal sialic acid residues from glycoconjugates. It is commonly used in molecular biology and biochemistry applications.
6
Pngase f by Roche
Sourced in Germany, United States, Switzerland, Australia
PNGase F is an enzyme that catalyzes the cleavage of asparagine-linked glycosidic linkages in glycoproteins and glycopeptides. It is commonly used in the analysis and characterization of glycoproteins.
7
O glycosidase by Roche
Sourced in Switzerland, Germany
O-glycosidase is an enzyme used in the laboratory setting. It functions to cleave O-glycosidic linkages, which are a type of chemical bond found in certain carbohydrate structures.
8
Sequencing grade trypsin by Promega
Sourced in United States, Germany, United Kingdom, Italy, France, Spain, Switzerland
Sequencing grade trypsin is a proteolytic enzyme used to cleave peptide bonds in protein samples, primarily for use in protein sequencing applications. It is purified to ensure high-quality, consistent performance for analytical processes.
9
N glycosidase f by New England Biolabs
Sourced in United States
N-glycosidase F is an enzyme that cleaves the bond between the asparagine residue and the first N-acetylglucosamine of N-linked glycans. It is commonly used in the analysis of glycoproteins.
10
Dithiothreitol (dtt) by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, Sao Tome and Principe, France, China, Switzerland, Macao, Spain, Australia, Canada, Belgium, Sweden, Brazil, Austria, Israel, Japan, New Zealand, Poland, Bulgaria
Dithiothreitol (DTT) is a reducing agent commonly used in biochemical and molecular biology applications. It is a small, water-soluble compound that helps maintain reducing conditions and prevent oxidation of sulfhydryl groups in proteins and other biomolecules.

More about "Glycoside Hydrolases"

Glycoside hydrolases, also known as carbohydrate-active enzymes (CAZymes), are a diverse group of enzymes that play a crucial role in the hydrolysis of glycosidic bonds in carbohydrates.
These versitile enzymes are involved in a wide range of biological processes, including biomass deconstruction, cell wall remodeling, and glycan metabolism.
Glycoside hydrolases are classified into different families based on their sequence and structural similarities.
Some well-known examples include PNGase F, which cleaves asparagine-linked (N-linked) glycosidic bonds; O-glycosidase, which removes O-linked glycans; Endo H, which cleaves high-mannose N-linked glycans; N-glycosidase F, which removes all types of N-linked glycans; and Neuraminidase, which removes terminal sialic acid residues.
Glycoside hydrolases have numerous applications in various industries, such as biofuel production, food processing, and therapeutic interventions.
Researchers can leverage tools like PubCompare.ai to efficiently identify the most accurate and reproducible protocols from the literature, preprints, and patents, optimizing their glycoside hydrolase studies and enhancing research efficiency and accuracy.
Sequencing grade trypsin and Dithiothreitol are also commonly used in conjunction with glycoside hydrolases for protein analysis and modification.
By understanding the diverse functions and applications of glycoside hydrolases, researchers can unlock new possibilities in carbohydrate-related research and development, contributing to advancements in fields like biotechnology, biochemistry, and healthcare.