Edward A. Bayer

ORCID: 0000-0001-7749-5150
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About
Contact & Profiles
Research Areas
  • Biofuel production and bioconversion
  • Enzyme Production and Characterization
  • Polysaccharides and Plant Cell Walls
  • Biotin and Related Studies
  • Advanced Cellulose Research Studies
  • Click Chemistry and Applications
  • Monoclonal and Polyclonal Antibodies Research
  • Microbial Metabolites in Food Biotechnology
  • Molecular Junctions and Nanostructures
  • Biochemical and Structural Characterization
  • Glycosylation and Glycoproteins Research
  • Microbial Metabolic Engineering and Bioproduction
  • Enzyme Structure and Function
  • Cellular transport and secretion
  • Genomics and Phylogenetic Studies
  • Legume Nitrogen Fixing Symbiosis
  • Catalysis for Biomass Conversion
  • Protein Structure and Dynamics
  • Bacterial Genetics and Biotechnology
  • Food composition and properties
  • Probiotics and Fermented Foods
  • Clostridium difficile and Clostridium perfringens research
  • Fungal and yeast genetics research
  • Signaling Pathways in Disease
  • Toxin Mechanisms and Immunotoxins

Weizmann Institute of Science
2015-2024

Ben-Gurion University of the Negev
2020-2024

Hudson Institute
2024

Israel Institute for Biological Research
2024

John Wiley & Sons (United States)
2024

Middle East Institute
2024

Liechtenstein Institute
2024

Merck Institute for Science Education
2024

Station Biologique de Roscoff
2021

Czech Academy of Sciences, Institute of Physics
2021

Greater understanding of the mechanisms contributing to chemical and enzymatic solubilization plant cell walls is critical for enabling cost-effective industrial conversion cellulosic biomass biofuels. Here, we report use correlative imaging in real time assess impact pretreatment, as well resulting nanometer-scale changes wall structure, upon subsequent digestion by two commercially relevant cellulase systems. We demonstrate that small, noncomplexed fungal cellulases deconstruct using...

10.1126/science.1227491 article EN Science 2012-11-22

The crystal structures of a deglycosylated form the egg-white glycoprotein avidin and its complex with biotin have been determined to 2.6 3.0 A, respectively. reveal amino acid residues critical for stabilization tetrameric assembly exceptionally tight binding biotin. Each monomer is an eight-stranded antiparallel beta-barrel, remarkably similar that genetically distinct bacterial analog streptavidin. As in streptavidin, involves highly stabilized network polar hydrophobic interactions....

10.1073/pnas.90.11.5076 article EN Proceedings of the National Academy of Sciences 1993-06-01

This chapter contains sections titled: Introduction Principle Preparation of Reactive Biotiny Derivatives Assays for Avidin and Biotin Purification Studies: Affinity Chromatography Localization Cytochemistry Miscellaneous Systems The Transport System: An Labeling Study Antibiotin Antibodies Conclusions

10.1002/9780470110461.ch1 article EN Methods of biochemical analysis 1980-02-13

The isolation and biochemical characterization of the extracellular form a cellulose-binding factor (CBF) from Clostridium thermocellum is described. CBF was isolated culture supernatant by two-step procedure which included affinity chromatography on cellulose gel filtration Sepharose 4B. homogeneous as determined immunoelectrophoresis, polyacrylamide electrophoresis, filtration, analytical ultracentrifugation analysis. found to complex exhibited molecular weight estimated at 2.1 million....

10.1128/jb.156.2.828-836.1983 article EN Journal of Bacteriology 1983-11-01

The adherence of Clostridium thermocellum, a cellulolytic, thermophilic anaerobe, to its insoluble substrate (cellulose) was studied. phenomenon determined be selective for cellulose. observed not significantly affected by various parameters, including salts, pH, temperature, detergents, or soluble sugars. A spontaneous adherence-defective mutant strain (AD2) isolated from the wild-type YS. Antibodies were prepared against bacterial cell surface and rendered specific cellulose-binding factor...

10.1128/jb.156.2.818-827.1983 article EN Journal of Bacteriology 1983-11-01

Humans, like all mammals, depend on the gut microbiome for digestion of cellulose, main component plant fiber. However, evidence cellulose fermentation in human is scarce. We have identified ruminococcal species microbiota populations that assemble functional multienzymatic cellulosome structures capable degrading cell wall polysaccharides. One these species, which strongly associated with humans, likely originated ruminant and was subsequently transferred to gut, potentially during...

10.1126/science.adj9223 article EN Science 2024-03-14

The bioconversion of lignocellulose has attracted global attention, due to the significant potential agricultural and forestry wastes as renewable zero-carbon resources urgent need for substituting fossil carbon. cellulosome system is a multi-enzyme complex produced by anaerobic bacteria, which comprises cellulases, hemicellulases, associated enzymatic non-enzymatic components that promote biomass conversion. To enhance their efficiency in degrading recalcitrant lignocellulosic matrices,...

10.1016/j.greenca.2024.01.003 article EN cc-by-nc-nd Green Carbon 2024-01-15

A library of 75 different chimeric cellulosomes was constructed as an extension our previously described approach for the production model functional complexes (Fierobe, H.-P., Mechaly, A., Tardif, C., Bélaı̈ch, Lamed, R., Shoham, Y., J.-P., and Bayer, E. A. (2001)<i>J. Biol. Chem.</i> 276, 21257–21261), based on high affinity species-specific cohesin-dockerin interaction. Each complex contained three protein components: (i) a scaffoldin possessing optional cellulose-binding module two...

10.1074/jbc.m207672200 article EN cc-by Journal of Biological Chemistry 2002-12-01

10.1016/0076-6879(90)84268-l article EN Methods in enzymology on CD-ROM/Methods in enzymology 1990-01-01

The cell surface topology of various gram-negative and -positive, anaerobic aerobic, mesophilic thermophilic, cellulolytic noncellulolytic bacteria was investigated by scanning electron microscopic visualization using cationized ferritin. Characteristic protuberant structures were observed on cells all strains. These appeared to be directly related the previously described exocellular cellulase-containing polycellulosomes Clostridium thermocellum YS (E. A. Bayer R. Lamed, J. Bacteriol....

10.1128/jb.169.8.3792-3800.1987 article EN Journal of Bacteriology 1987-08-01

The properties of the cellulosome (the cellulose-binding, multicellulase-containing protein complex) in Clostridium thermocellum were examined by comparing cellulase systems derived from wild type and an adherence-defective mutant. growth conditions--specifically, either on cellulose (Avicel) or cellobiose as insoluble soluble carbon sources, respectively--were found to be critical distribution mutant system: cellobiose-grown (in contrast type) lacked its surface produced only minor...

10.1128/jb.163.2.552-559.1985 article EN Journal of Bacteriology 1985-08-01
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