Enzymatic Plastic Bioremediation Simulator

Reactor Conditions

Enzyme concentration [E] 120 nM

Temperature 45 °C

pH 8.0

PET crystallinity 30%

Reactor Readouts

0.0% PET degraded100.0% remaining

Degradation rate

0.0 mg/L/h

Monomers released

0.00 mM

Elapsed (reactor time)

0.0 h

Est. time to 90% clean

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How it works

Real PETases (e.g. the engineered leaf-branch compost cutinase variants used at industrial scale by companies like Carbios) don't dissolve plastic uniformly — they attack the surface of each solid fragment and eat inward, exactly like a leaching or combustion particle. That's a shrinking-core model: each fragment's volume shrinks at a rate set by its current surface area, not its volume.

dV/dt = −k_eff · A(V),   A(V) = c · V^(2/3)

k_eff = k₀ · [E]/(K_m+[E]) · f_T(T) · f_pH(pH) · (1 − x_c)^1.5

f_T(T)  = exp(−((T−45)/12)²) · (1 − sigmoid((T−68)/3))   [thermal optimum, then denaturation]
f_pH(pH)= exp(−((pH−8)/1.6)²)                              [enzyme active-site protonation]
x_c     = crystallinity fraction (crystalline PET packs tighter, resists attack)

[E] — more enzyme molecules loaded onto the surface saturates like Michaelis-Menten enzyme kinetics: doubling [E] from 200→400 nM helps far less than 0→200 nM.
Temperature — faster chemistry up to ~45 °C, then the protein itself starts unfolding; push past ~68 °C and the enzyme denatures and the rate collapses.
pH — the enzyme's catalytic residues need the right protonation state; most engineered PETases peak near pH 7.5–8.5.
Crystallinity — amorphous PET (post-consumer bottles after a heat/quench pre-treatment) degrades far faster than the crystalline PET in unprocessed rigid packaging.

Every fragment tracks its own volume; each frame the surface-limited rate above shrinks it, monomer release (terephthalic acid + ethylene glycol) is added in proportion to the volume lost, and the tank readouts aggregate every fragment in the reactor.

PET fragments (shrinking) Enzyme molecules

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