Search bioRxiv⌕ Search

bioRxiv · 10.1101/411819

Developing a unique medical-grade honey which maximizes glucose oxidase activity

Abstract

In the fight against cancer and infection, honey is a compelling solution by virtue of its unique chemical composition; however, current medical-grade honeys are expensive and limited in their scope. In this study, a novel medical-grade honey was developed by maximizing the activity of glucose oxidase (GOX), an enzyme in honey that synthesizes hydrogen peroxide; maximization was done by neutralizing the effects of catalase and methylglyoxal (MGO), compounds in honey that interfere with H2O2 accumulation. Expressed GOX activity was quantified via H2O2 accumulation in honey after catalase, MGO, or both were inhibited. Results indicate the honeys tested have significant quantities of H2O2 inhibitors, greatly affecting expressed GOX activity; neutralization resulted in at least a 100% increase in H2O2 accumulation in all honeys. Blueberry honey with catalase inhibition by EGCG saw a 938% increase in H2O2 accumulation, reaching nearly three times the H2O2 accumulation in current medical grade honey for a tenth of the cost. This research presents a novel and readily reproducible method for maximizing H2O2 accumulation in any honey through neutralization of GOX inhibitors. GOX activity enhancement, combined with honeys diverse antioxidants, enables the emergence of global low-cost medical-grade honeys with immense potential to revolutionize cancer and infection treatment.\n\nThis paper is based on work presented at the Regional Science and Engineering Fair on March 15, 2018 at Riverside High School (Loudoun County, Virginia), the Virginia State Science and Engineering Fair on April 14, 2018 at the Virginia Tech Carilion School of Medicine (Roanoke, Virginia).\n\nAuthor SummaryWith cancer and post-operative infections on the rise, a natural, low-cost alternative treatment is necessary. Honey is an ideal candidate due to its diverse antioxidants and glucose oxidase, an enzyme that produces hydrogen peroxide. The purpose of this research was to maximize glucose oxidase activity by neutralizing compounds that interfere with H2O2 accumulation. This research yielded medical-grade honeys that are economical and more effective than current ones, presenting a novel method that is reproducible on a large scale, scalable to different needs, and applicable to any honey to create low-cost medical-grade honeys that can revolutionize cancer and infection treatment globally.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Li, Z., Parikh, R.. 2018-09-10. Developing a unique medical-grade honey which maximizes glucose oxidase activity. https://doi.org/10.1101/411819

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

The intrinsically disordered N-terminal region of eIF5B nucleates RNA-driven phase separation

Recently, we found that eukaryotic Initiation Factor 5B (eIF5B) forms cytoplasmic puncta under conditions of cellular stress and that the puncta formation drives an increase in alternative translation initiation. The formation of these puncta depends on the intrinsically disordered N-terminal region of eIF5B (eIF5B-NTR). To address the driving force behind this observation, we reconstituted a purified, binary, in vitro system to study the phase separation potential of the eIF5B-NTR. Utilizing this system, we show that eIF5B-NTR forms RNA-driven condensates at physiological concentrations. Furthermore, we defined the properties of the eIF5B condensates and the amino acid sequence requirements of this polypeptide to form complex liquid-liquid condensates. Truncation mapping identified a central arginine-rich core (residues ~200-400) that drives condensation but forms nearly static droplets in the absence of the rest of the polypeptide. Finally, we tested this model in cells to determine if the in vitro observations apply to the complex cellular environment.

biochemistry↗

Structural basis of ribosomal RNA repair by RtcB2

Ribotoxins disable ribosomes by cleaving ribosomal RNA, but how repair enzymes recognize and restore these damaged machines remains unclear. Here, we report three cryo-electron microscopy structures of the RNA ligase RtcB2 bound to damaged Escherichia coli 30S subunits. An extended interface stabilizes the ribosomal head and decoding-center scaffold while positioning the cleaved 3'-phosphate end within the catalytic pocket. Two structures contain enzyme-linked guanosine monophosphate, whereas the third captures its transfer to the RNA. RNA activation accompanies RtcB2 reorientation and entry of the 5'-hydroxyl-containing segment into an adjacent cleft. Comparisons with assembled ribosomes reveal structural barriers to substrate access. These structures connect recognition of a damaged ribosome to chemical activation of its RNA for repair.

biochemistry↗

Enhancers Silence Coupled-coding RNAs in Animals

The exact working mechanism and biogenesis of regulatory non-coding RNAs (rncRNAs), including enhancer RNAs (eRNAs), microRNAs (miRNAs), piRNAs, small interfering RNAs (siRNAs), transposons, and other non-coding RNAs, remain enigmatic. Conversely, the unique transcriptional regulation mechanism that differentiates animals from simple unicellular organisms remains elusive in life sciences. We find that regulatory non-coding genes are independent transcription units marked with arginine methylation of nucleosomes within their gene bodies, which is regulated by JMJD5. Enhancer RNAs are similar to those of other regulatory RNAs in targeting the 3-prime UTRs of coupled coding RNAs. All regulatory RNA genes share transcription factors with their target coding genes, both of which are regulated by promoter-proximal RNA Polymerase II pausing and may control the development of animals. Temporal and spatial coding genes and regulatory non-coding genes are intrinsically coupled in animals.

biochemistry↗