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Related Concept Videos

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
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Strain improvement is a foundational strategy in industrial microbiology aimed at maximizing microbial productivity, particularly because natural isolates typically yield commercially valuable products in very low concentrations. Although optimizing the culture medium and environmental conditions can improve yields, these adjustments are inherently limited by the organism’s genetic potential. As a result, the focus shifts toward genetic modifications to enhance biosynthetic capacity. The...
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Heterogeneous Catalysis

Heterogeneous catalysis involves a catalyst in a different phase from the reactants. It is a process where the catalyst and the reactants are in distinct phases, typically solid and gas or liquid.Most heterogeneous catalysts are metals, metal oxides, or acids. The list includes transition metals like iron (Fe), cobalt (Co), nickel (Ni), palladium (Pd), platinum (Pt), chromium (Cr), manganese (Mn), tungsten (W), silver (Ag), and copper (Cu). These metals possess partially vacant d orbitals that...

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Engineering bifunctional laccase-xylanase chimeras for improved catalytic performance.

Lucas F Ribeiro1, Gilvan P Furtado, Marcos R Lourenzoni

  • 1Departamento de Bioquímica e Imunologia, Universidade de São Paulo, Ribeirão Preto-SP, 14049-900, Brazil.

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Area of Science:

  • Enzyme Engineering
  • Biocatalysis
  • Protein Chemistry

Background:

  • Enzymes with multiple catalytic activities are valuable for industrial processes.
  • Combining xylanase and laccase activities in a single enzyme offers potential for streamlined biotransformations.

Purpose of the Study:

  • To design and characterize bifunctional enzymes with combined xylanase and laccase activities.
  • To investigate the impact of gene fusion on enzyme kinetics, structure, and catalytic efficiency.

Main Methods:

  • Gene fusion of Bacillus subtilis cotA (laccase) and xynA (xylanase) genes.
  • Construction of chimeric enzymes using wild-type and thermostable xylanase variants.
  • Biochemical assays, kinetic measurements, molecular dynamics simulations, and biophysical characterization (SAXS, UV-Vis, EPR spectroscopy).

Main Results:

  • Chimeric enzymes retained parental catalytic domains with minor shifts in optima.
  • Laccase activity exhibited a 2-fold increase in catalytic efficiency (kcat/Km) in both chimeras.
  • Structural analysis revealed domain proximity and altered loop structures, enhancing active site accessibility and copper ion exposure.

Conclusions:

  • Successful engineering of bifunctional xylanase-laccase enzymes.
  • Inter-domain interactions in chimeras positively influence laccase activity and accessibility.
  • Designed enzymes show promise for applications requiring combined enzymatic functions.