3,000 Units at 50oC
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|Content:||3,000 Units at 50oC|
|Formulation:||In 3.2 M ammonium sulphate|
|Stability:||Minimum 1 year at 4oC. Check vial for details.|
|Enzyme Activity:||Other Activities|
|Synonyms:||alpha-L-rhamnosidase; alpha-L-rhamnoside rhamnohydrolase|
|Concentration:||Supplied at ~ 1,500 U/mL|
|Expression:||Recombinant from a Prokaryotic source|
|Specificity:||Hydrolysis of terminal non-reducing α-L-rhamnose residues in α-L-rhamnosides.|
|Specific Activity:||~ 110 U/mg (50oC, pH 6.5 on p-nitrophenyl-α-L-rhamnoside)|
|Unit Definition:||One Unit of α-L-rhamnosidase activity is defined as the amount of enzyme required to release one µmole of p-nitrophenol (pNP) per minute from p-nitrophenyl-α-rhamnoside (5 mM) in sodium phosphate buffer (100 mM), pH 6.5 at 50oC.|
|Application examples:||Applications in carbohydrate and biofuels research.|
High purity recombinant α-Rhamnosidase (prokaryote) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
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The Search for Cryptic L-Rhamnosyltransferases on the Sporothrix schenckii Genome.
Mora-Montes, H. M., García-Gutiérrez, K., García-Carnero, L. C., Lozoya-Pérez, N. E. & Ramirez-Prado, J. H. (2022). Journal of Fungi, 8(5), 529.
The fungal cell wall is an attractive structure to look for new antifungal drug targets and for understanding the host-fungus interaction. Sporothrix schenckii is one of the main causative agents of both human and animal sporotrichosis and currently is the species most studied of the Sporothrix genus. The cell wall of this organism has been previously analyzed, and rhamnoconjugates are signature molecules found on the surface of both mycelia and yeast-like cells. Similar to other reactions where sugars are covalently linked to other sugars, lipids, or proteins, the rhamnosylation process in this organism is expected to involve glycosyltransferases with the ability to transfer rhamnose from a sugar donor to the acceptor molecule, i.e., rhamnosyltransferases. However, no obvious rhamnosyltransferase has thus far been identified within the S. schenckii proteome or genome. Here, using a Hidden Markov Model profile strategy, we found within the S. schenckii genome five putative genes encoding for rhamnosyltransferases. Expression analyses indicated that only two of them, named RHT1 and RHT2, were significantly expressed in yeast-like cells and during interaction with the host. These two genes were heterologously expressed in Escherichia coli, and the purified recombinant proteins showed rhamnosyltransferase activity, dependent on the presence of UDP-rhamnose as a sugar donor. To the best of our knowledge, this is the first report about rhamnosyltransferases in S. schenckii.Hide Abstract
Interaction analysis of commercial graphene oxide nanoparticles with unicellular systems and biomolecules.
Domi, B., Rumbo, C., García-Tojal, J., Elena Sima, L., Negroiu, G. & Tamayo-Ramos, J. A. (2020). International Journal of Molecular Sciences, 21(1), 205.
The ability of commercial monolayer graphene oxide (GO) and graphene oxide nanocolloids (GOC) to interact with different unicellular systems and biomolecules was studied by analyzing the response of human alveolar carcinoma epithelial cells, the yeast Saccharomyces cerevisiae and the bacteria Vibrio fischeri to the presence of different nanoparticle concentrations, and by studying the binding affinity of different microbial enzymes, like the α-l-rhamnosidase enzyme RhaB1 from the bacteria Lactobacillus plantarum and the AbG β-d-glucosidase from Agrobacterium sp. (strain ATCC 21400). An analysis of cytotoxicity on human epithelial cell line A549, S. cerevisiae (colony forming units, ROS induction, genotoxicity) and V. fischeri (luminescence inhibition) cells determined the potential of both nanoparticle types to damage the selected unicellular systems. Also, the protein binding affinity of the graphene derivatives at different oxidation levels was analyzed. The reported results highlight the variability that can exist in terms of toxicological potential and binding affinity depending on the target organism or protein and the selected nanomaterial.Hide Abstract
Ma, F., Wang, D., Zhang, Y., Li, M., Qing, W., Tikkanen-Kaukanen, C., Liu, X. & Bell, A. E. (2018). Food Chemistry, 245, 13-21.
The mucilage polysaccharides from Dioscorea opposita (DOMP) were extracted and treated with a single/dual enzymatic hydrolysis. The characterisation and viscosity were subsequently investigated in this study. DOMP obtained 62.52% mannose and 23.45% glucose. After single protease and trichloroacetic acid (TCA) treatments, the mannose content was significantly reduced to 3.96%, and glucose increased from 23.45% to 45.10%. Dual enzymatic hydrolysis also decreased the mannose and glucose contents to approximately 18%–35% and 7%–19%, respectively. The results suggest that enzymatic degradation could effectively remove the protein from DOMP accompanied by certain polysaccharides, especially mannose. The molecular weight, surface morphology, viscosity and particle sizes were measured. Enzymatic hydrolysis reduced molecular weight, decreased the viscosity, and increased the particle sizes, which indicates that the characterisations of DOMP samples were altered as structures changed. This study was a basic investigation into characterisation of DOMP to contribute to the processing of food by-products.Hide Abstract
Potocká, E. K., Mastihubová, M., Čičová, I. & Mastihuba, V. (2017). Monatshefte für Chemie-Chemical Monthly, 149(1), 167-174.
Free rutinose was prepared by enzymatic hydrolysis of rutin using defatted seed meal from tartary buckwheat. This disaccharide was used as substrate in spectrophotometric assay of α-L-rhamnosidase. The assay is based on hydrolysis of rutinose and subsequent determination of released glucose by a standard glucose oxidase assay kit. The method is easy to perform and requires no expensive equipment. The assay was applied in α-L-rhamnosidase estimation in ten commercial enzyme preparations and compared with standard assay on chromogenic substrate.Hide Abstract
Mueller, M., Zartl, B., Schleritzko, A., Stenzl, M., Viernstein, H. & Unger, F. M. (2017). Bioprocess and Biosystems Engineering, 1-8.
Bioavailability of flavonoids is low, especially when occurring as rhamnoglucosides. Thus, the hydrolysis of rutin, hesperidin, naringin and a mixture of narcissin and rutin (from Cyrtosperma johnstonii) by 14 selected probiotics was tested. All strains showed rhamnosidase activity as shown using 4-nitrophenyl α-L-rhamnopyranoside as a substrate. Hesperidin was hydrolysed by 8-27% after 4 and up to 80% after 10 days and narcissin to 14-56% after 4 and 25-97% after 10 days. Rutin was hardly hydrolysed with a conversion rate ranging from 0 to 5% after 10 days. In the presence of narcissin, the hydrolysis of rutin was increased indicating that narcissin acts as an inducer. The rhamnosidase activity as well as the ability to hydrolyse flavonoid rhamnoglucosides was highly strain specific. Naringin was not hydrolysed by rhamnosidase from probiotics, not even by the purified recombinant enzyme, only by fungal rhamnosidase. In conclusion, rhamnosidases from the tested probiotics are substrate specific cleaving hesperidin, narcissin and to a small extent rutin, but not naringin.Hide Abstract
Kim, D. Y., Yeom, S. J., Park, C. S. & Kim, Y. S. (2016). Biotechnology Letters, 38(10), 1775-1780.
Objectives: To optimize conversion of rutin to isoquercetin by commercial α-L-rhamnosidase using high hydrostatic pressure (HHP). Results: The de-rhamnosylation activity of α-L-rhamnosidase for isoquercetin production was maximal at pH 6.0 and 50°C using HHP (150 MPa). The enzyme showed high specificity for rutin. The specific activity for rutin at HHP was 1.5-fold higher than that at atmospheric pressure. The enzyme completely hydrolysed 20 mM rutin in tartary buckwheat extract after 2 h at HHP, with a productivity of 10 mM h−1. The productivity and conversion were 2.2- and 1.5-fold higher at HHP than at atmospheric pressure, respectively. Conclusions: This is the first report concerning the enzymatic hydrolysis of isoquercetin in tartary buckwheat at HHP.Hide Abstract