3.4.
2 Polyethylene (PE)
PE is the world’s most produced plastic, about 30% of global output, and a
polyolefin made entirely of carbon–carbon backbone bonds, which puts it
among the toughest substrates for enzymes. Its biodegradation runs in
sequence. Abiotic oxidation (UV, ozone, or heat) first adds carbonyl, hydroxyl,
and carboxylate groups that lower average molecular weight and raise
hydrophilicity. Microbial oxidases (laccases, peroxidases, oxygenases) then
extend the oxidative attack under aerobic conditions. The oxidised fragments,
hydrocarbon chains carrying terminal or internal oxo-groups, become
accessible to β-oxidation. Finally, β-oxidation trims the chains down to acetyl-
CoA units that feed the TCA cycle.
Bacterial PE degraders include Ideonella sakaiensis (with limited PE activity),
Bacillus safensis, Brevibacillus brevis, Rhodococcus ruber, and members of the
Alcanivorax genus. Pseudomonas aeruginosa is among the most studied; it
makes biosurfactants (rhamnolipids) that emulsify PE and open up more
surface for enzymes. Alcanivorax borkumensis, common in oil-polluted
seawater, expresses alkane hydroxylases of the CYP153 and AlkB families that
hydroxylate aliphatic chains at their ends, a natural preadaptation to PE
degradation.
3.4.3 Polystyrene (PS)
PS is an aromatic vinyl polymer, and its benzene rings create a double
problem: the aromatic system is chemically stable and needs oxidative ring-
opening, while the carbon backbone resists hydrolysis just as firmly. Mealworm
larvae of Tenebrio molitor were famously shown to metabolise PS, and later
work traced the activity to gut bacteria, especially Exiguobacterium sp. strain
YT2 and members of the Enterobacteriaceae. Among free-living bacteria, PS
degradation has been attributed to Pseudomonas putida, Citrobacter sp., and
Rhodococcus ruber, with laccases and monooxygenases identified as the main
enzymes.
The proposed route for PS mineralisation in bacteria runs as follows: oxidative
attack by laccase or monooxygenase generates styrene oxide and other epoxide
intermediates; styrene oxide hydrolase opens the ring to give
phenylacetaldehyde; phenylacetaldehyde dehydrogenase converts that to
phenylacetic acid; and the phenylacetic acid (PAA) pathway then takes over,
using a multicomponent PAA oxygenase system that hydroxylates the aromatic
ring before cleaving it. Under fungal action, lignin-oxidising peroxidases supply
the oxidative start, though fungal PS degradation tends to run slower than
fungal PE degradation.
3.4.4 Polypropylene (PP) and PVC
1
Polypropylene has the same carbon–carbon backbone as PE but adds methyl
side groups that crowd the chain and make it even harder for enzymes to
reach. PP degradation has been reported in Bacillus cereus, Bacillus gottheilii,
and Rhodococcus sp., usually after UV or thermal pre-oxidation, and the
mechanisms mirror PE degradation but run slower because of the methyl
branching. PVC brings a different complication: plasticisers, usually phthalate
esters, are often present in quantity and may be degraded before the polymer
backbone is touched. The heavily chlorinated PVC backbone resists both
hydrolytic and oxidative enzymes; anaerobic bacteria (Dehalococcoides
mccartyi) can carry out reductive dechlorination, but full mineralisation of the
polymer remains out of reach.
4. Microbial Diversity in Plastic Degradation
4.1 Bacterial Degraders
Plastic-degrading bacteria are spread across a wide phylogenetic range, which
reflects both the many independent evolutionary origins of this ability and the
variety of polymer chemistry it has to handle. Within the Proteobacteria,
Pseudomonas species are among the most studied: P. putida, P. aeruginosa,
and P. fluorescens grow on a range of plastic substrates and their plasticisers,
helped by a versatile set of oxygenases, dehydrogenases, and biosurfactant-
producing genes. Pseudomonas species can metabolise styrene monomers
through the styrene catabolism pathway (sty genes), converting styrene to
phenylacetyl-CoA and on to acetyl-CoA.
Within the Firmicutes, Bacillus species, particularly Bacillus subtilis, B. cereus,
and B. gottheilii, have been reported as PE and PP degraders that form sturdy
biofilms on plastic surfaces and secrete a range of oxidative enzymes. Bacillus
safensis has drawn attention for degrading PE better after plasma activation,
where added surface oxidation makes enzymatic colonisation easier. Bacillus
rhizobacteria have also degraded PET in soil, a reminder that soil microbiota
matter for terrestrial plastic pollution.
Actinomycetes, particularly Rhodococcus, Streptomyces, and Mycobacterium,
stand out for catabolising long-chain hydrocarbons and aromatic compounds,
which makes them important polyolefin degraders. Rhodococcus ruber is
especially well characterised for PE degradation, and its genome encodes a
deep set of alkane hydroxylases, aldehyde dehydrogenases, and acyl-CoA
synthetases consistent with chain-shortening. Ideonella sakaiensis, the model
PET degrader, belongs to the order Burkholderiales in the Betaproteobacteria
and has no characterised ability to degrade polyolefins.
2
Table 2: Representative Bacterial Species and Their Plastic Degradation
Profiles
Bacterial Species Phylum Target Main Enzymes
Polymer(s)
Ideonella sakaiensis Betaproteobacteria PET PETase, MHETase
Pseudomonas putida Gammaproteobacteri PS, PU, PE Laccase, oxygenase,
a lipase
Bacillus subtilis Firmicutes PE, PS, PU Laccase, lipase,
protease
Rhodococcus ruber Actinomycetes PE Alkane hydroxylase
(CYP450)
Bacillus cereus Firmicutes PP, PE Oxidase,
dehydrogenase
Alcanivorax Gammaproteobacteri PE, alkanes AlkB hydroxylase,
borkumensis a CYP153
Acinetobacter Gammaproteobacteri PET, PE Esterase, lipase
baumannii a
Streptomyces sp. Actinomycetes PE, PU Peroxidase, laccase
Table 2: Representative bacterial species involved in microplastic degradation, with their
phylogenetic classification, target polymers, and the enzymes implicated in biodegradation.
4.2 Fungal Degraders
Fungi have long been the main decomposers of stubborn natural polymers such
as lignin, cellulose, and chitin, because they secrete oxidative enzymes at high
titre, above all laccases, lignin peroxidases, and manganese peroxidases. That
natural toolkit leaves many fungi preadapted to attack synthetic polymers, and
a growing body of work confirms real fungal degradation of PE, PVC, PS, and
PU.
White-rot Basidiomycetes, including Trametes versicolor, Pleurotus ostreatus,
and Phanerochaete chrysosporium, are the most studied. Trametes versicolor
laccase binds PE more tightly than any other commonly tested ligninolytic
enzyme in molecular docking studies. The lignin peroxidase and manganese
peroxidase systems of Phanerochaete chrysosporium, central to breaking down
lignin, have shown promise in oxidising PE and PS. One advantage is
structural: fungi grow penetrating hyphae that physically break up the plastic
surface while delivering oxidative enzymes to freshly exposed polymer chains,
a combined mechanical and enzymatic attack that unicellular bacteria cannot
manage.
Ascomycete fungi, including Aspergillus niger, A. tubingensis, Penicillium
simplicissimum, and Fusarium solani, degrade PE, PU, and PET. Their
esterases and cutinases are well suited to polyester degradation. Fusarium
3
solani cutinase (FsC) was among the first characterised PET-degrading
enzymes and is still a useful structural reference for engineering work. The
marine-adapted fungus Pestalotiopsis microspora was reported, in a much-cited
study, to degrade PU anaerobically using a serine hydrolase, a rare case of
anaerobic plastic degradation.
Many fungal degradation studies share a weakness worth naming: the weight-
loss percentages they report, the usual metric, tend to be small (1–10% over
weeks to months), and they often do not separate true degradation from
surface colonisation and biomass deposition. Confirming fungal mineralisation
rigorously calls for molecular weight distribution analysis (GPC/SEC), surface
functional group analysis (FTIR, XPS), and isotope labelling.
4.3 Microbial Consortia versus Pure Cultures
Most early plastic degradation studies used isolated pure cultures, which kept
experiments tractable and mechanisms clear. But natural plastic degradation is
carried out by microbial consortia, communities in which different species
bring complementary metabolic abilities and together degrade more, and more
completely, than any single species can.
Consortia hold several advantages over pure cultures. They divide the labour,
with one species oxidising the surface, another running β-oxidation on chain
fragments, and a third mineralising aromatic intermediates. They are more
stable, riding out environmental swings and resisting invasion by competitors.
They cross-feed, so the by-products of one species feed another and keep the
community active for longer. And they pool a wider set of enzymes, which lets
them attack several polymer types at once.
Synthetic ecology, the deliberate design of small defined consortia with set
complementary roles, is a promising way to engineer highly active plastic-
degrading communities. The EU Horizon 2020 MIX-UP project pursued this
idea, aiming to build engineered consortia that break down mixed plastic waste
and turn the resulting monomers into value-added chemicals. Work like this
demands a careful understanding of how species interact, how metabolic flux
moves through the community, and how stable that community stays under
realistic conditions.
Summary: Microbial consortia degrade plastic more efficiently than pure
cultures because their enzymatic functions complement one another, their
cross-feeding networks sustain activity, and the community as a whole stays
stable. Synthetic ecology, the rational design of minimal consortia, is a
frontier approach for industrial-scale plastic bioremediation.
4
5. Toward a Circular Bioeconomy: Monomer Valorisation
5.1 Upcycling PET-Derived Monomers
A circular bioeconomy turns waste into useful resources through biological
processes, cutting both resource extraction and waste, and it is here that
enzymatic plastic degradation earns its place. The discovery that an enzymatic
cascade can fully depolymerise PET to TPA and EG changed how people think
about plastic waste. Rather than a liability to dispose of, it becomes a carbon
feedstock for producing useful chemicals.
TPA, the aromatic diacid monomer of PET, is a valuable commodity in its own
right, used to make PET, polyurethanes, and polyamides. Chemical recycling of
TPA from PET is well established, but enzymatic depolymerisation has
advantages: it runs at lower temperatures, gives higher product purity without
the coloured contaminants of glycolysis-based chemical depolymerisation, and
produces aqueous product streams that biology can work with. Beyond being
repolymerised into virgin-quality PET, TPA can serve as a carbon source for
microbial synthesis of other valuable compounds.
Engineered microbial strains can convert TPA and EG into a range of high-
value products. Metabolic engineering of Pseudomonas putida, a strain well
suited to aromatic compound catabolism, has redirected TPA catabolism
toward β-ketoadipate, muconic acid (a precursor for bio-based nylon and adipic
acid), and protocatechuic aldehyde. Ethylene glycol can be metabolised by
Escherichia coli and Halomonas strains to make glycolic acid (a platform
chemical for biodegradable polymers) or glyoxylate (a precursor for C2
compound metabolism). In one study, engineered Yarrowia lipolytica secreting
PETase was co-cultivated with EG-consuming E. coli in a two-organism system
that coupled PET depolymerisation with EG valorisation, a clean proof of
concept for integrated bio-upcycling.
Using PET-derived TPA and EG as substrates for PHA (polyhydroxyalkanoate)
production is one of the more appealing routes from a circular-economy view.
PHAs are biodegradable polyesters that many bacteria, including Cupriavidus
necator and recombinant Pseudomonas strains, build intracellularly under
carbon-rich, nitrogen-limited conditions. If plastic waste can be turned into
PHA through enzymatic depolymerisation followed by microbial fermentation,
the result is a closed loop: a non-biodegradable plastic becomes a
biodegradable one.
Figure 2: Circular bioeconomy framework for microplastic valorisation, showing the stages
from plastic waste through enzymatic degradation to monomer recovery and biological
upcycling into high-value products.
5
5.2 Valorisation of Polyolefin Degradation Products
Valorising polyolefin degradation products is harder than valorising PET,
because oxidative degradation of PE, PP, and PS yields mixed batches of partly
oxidised intermediates, carboxylic acids, alcohols, aldehydes, ketones, and
aromatics, whose makeup shifts with polymer type, degree of pre-oxidation,
and the enzymatic toolkit of the degrading community. Even so, several studies
show these intermediates can feed the production of useful compounds.
Long-chain fatty acids and dicarboxylic acids from PE oxidation can be routed
into PHA biosynthesis by Cupriavidus necator and related
polyhydroxyalkanoate producers. The propylene and ethylene fragments
released from PP and PE could in principle serve as feedstocks for chemical re-
polymerisation or as fuels. Styrene from PS degradation is itself a valuable
monomer; if PS could be selectively depolymerised to styrene in high yield
instead of being fully mineralised, that would be a particularly useful form of
chemical recycling, though PS recalcitrance and styrene toxicity to many
microorganisms still stand in the way.
5.3 Bioplastic Synthesis from Plastic Waste
One of the clearest expressions of the circular bioeconomy is turning fossil-
derived plastic waste into bioplastics through integrated bio-upcycling
platforms, and several routes have been demonstrated at laboratory scale.
Muconic acid, made from TPA via the protocatechuate branch of the β-
ketoadipate pathway in engineered P. putida, can be hydrogenated to adipic
acid, a monomer for nylon-6,6, or polymerised directly into bio-based semi-
aromatic polyesters. Vanillic acid and other phenolic compounds released
during aromatic plastic degradation can serve as substrates for biosynthesising
coniferyl alcohol and lignin-like polymers used in advanced materials.
Engineered E. coli strains have produced lycopene, violacein, and other high-
value pigments and nutraceuticals from PET-derived carbon, which shows
plastic waste can act as a renewable feedstock for specialty chemicals. The
economics make sense: even where degradation is slow and energy-hungry at
current scales, the value of the bio-based products can offset processing costs
and give investors a reason to fund plastic bioremediation infrastructure.
The European Bioeconomy Alliance (EUBA) has set a target for 10% of all EU
packaging to come from biobased origins by 2030, and the MIX-UP project
(MIXed plastics biodegradation and UPcycling using microbial communities)
took on the specific problem of processing mixed plastic waste through
enzymatic and microbial routes. These frameworks show a growing recognition
at institutional and regulatory levels that biological plastic valorisation can help
6
move plastics from a linear make-use-dispose model to a circular make-use-
recover-remake one.
6. Factors Governing Enzymatic Degradation Efficiency
6.1 Polymer Properties
The physical and chemical properties of the plastic itself usually set the pace of
enzymatic degradation and are often the real bottleneck in practice. The
properties that matter most are molecular weight, crystallinity, surface
hydrophobicity, additive content, and the chemical structure of the backbone.
Molecular weight shapes chain mobility and the physical state of the polymer.
High molecular weight polymers are more viscous, and below their glass
transition temperature (Tg) the chain segments barely move, which keeps
enzymes away from the bonds they need to cut. As molecular weight drops, for
example through abiotic pre-treatment, the polymer opens up to enzymatic
attack. Crystallinity matters most for PET: in crystalline domains the chains
pack tightly and line up, shutting enzymes out of the ester bond sites. Raising
the amorphous fraction, say by heating above Tg and quench-cooling, speeds
up PETase considerably.
Additives in commercial plastics, including UV stabilisers, antioxidants, flame
retardants, plasticisers, and pigments, can suppress microbial growth and
enzyme activity. They can also do the opposite, acting as preferred carbon
sources that keep microbial communities alive on an otherwise recalcitrant
substrate. Because post-consumer plastic waste carries such variable additive
profiles, building standardised biodegradation protocols is difficult, and
extrapolating from pure-polymer studies to the real world is risky.
6.2 Environmental Conditions
Temperature, pH, UV history, salinity, oxygen, and nutrients all change how
fast enzymes degrade plastic in the field. Temperature stands out. Most
characterised plastic-degrading enzymes have optima between 30°C and 75°C,
but marine surface waters average around 20°C and deep soils can sit at 5–
10°C, so enzyme activity drops sharply in those settings. This cold gap may
explain an apparent paradox: microplastics persist for centuries in cold oceans
even though microbial biofilms colonise them.
UV irradiation is an important abiotic pre-treatment for polyolefins. Solar UV
breaks chains and adds carbonyl groups through Norrish type I and II
photooxidation, lowering average molecular weight, raising surface
hydrophilicity, and creating functional groups that give enzymes a foothold.
Without UV pre-treatment, many bacterial and fungal degraders show almost
7
no activity on PE and PP. In the open ocean, then, UV weathering of floating
debris may be a precondition for microbial attack, making degradation a two-
step abiotic-then-biotic process.
Salinity and nutrient supply shape both plastisphere composition and
enzymatic activity. Nutrient-rich coastal and estuarine waters support denser,
more active plastisphere communities than nutrient-poor open ocean.
Biostimulation, adding limiting nutrients such as nitrogen and phosphorus to
spur native degraders, has been tried as a way to speed up in situ degradation,
with some success in laboratory mesocosms.
6.3 Enzyme Engineering and Protein Design
Rational protein engineering and directed evolution have produced large gains
in the activity and stability of plastic-degrading enzymes, most of all for
PETase. The main strategies are: active-site mutagenesis to tighten substrate
binding or shift product specificity; disulphide bond engineering to raise
thermostability; surface charge changes to alter how the enzyme adsorbs to
plastic; and fusion designs that create bifunctional enzymes or attach
carbohydrate-binding modules to improve surface attachment.
FAST-PETase (functional, active, stable, and tolerant PETase), built with a
machine-learning model trained on sequence-function relationships, carries five
mutations relative to wild-type PETase and shows much stronger activity from
30°C to 50°C, enough to degrade post-consumer coloured PET at moderate
temperatures. The thermostable cutinase variant LCC-ICCG, with added salt
bridges and loop stabilisation, depolymerises highly crystalline industrial PET
at 72°C with high conversion, the closest thing yet to an industrially viable
PET-degrading enzyme.
Computational protein design, including Rosetta-based structure prediction,
AlphaFold2-guided stability engineering, and large-language-model sequence
generation, is widening the toolkit fast. Predicting enzyme structure at atomic
resolution lets researchers design mutations that improve active-site geometry,
substrate fit, and product release, cutting the design-build-test cycle from years
to weeks. Paired with high-throughput screening and directed evolution in
robotic systems, these methods should yield much-improved plastic-degrading
enzymes over the next five to ten years.
7. Challenges and Limitations
The mechanisms are now well understood, but several obstacles still stand
between the laboratory and the scale needed to address the global microplastic
8
problem. They span biology, chemistry, engineering, economics, and
regulation.
The biggest biological obstacle is how recalcitrant the most common plastics
are. Polyethylene, polypropylene, and polystyrene together make up over 60%
of global production, yet none carry hydrolysable bonds, so their enzymatic
degradation runs orders of magnitude slower than PET’s. The best PE-
degrading microorganisms manage weight losses of only a few percent over
weeks of incubation, far short of what remediation would require. The
thermodynamic and kinetic barriers to cleaving C–C bonds under mild
conditions set a ceiling that protein engineering alone cannot lift.
Enzyme thermostability is a second biological obstacle. Most characterised
plastic-degrading enzymes are mesophilic, peaking near 30–40°C and
inactivating quickly above that. Industrial processes tend to run hot to speed
reactions and limit contamination, so building variants that stay active at 60–
80°C while keeping access to the plastic surface is technically hard. LCC-ICCG
shows thermostabilisation is achievable for cutinases, but no one has yet
repeated it for the oxidative enzymes needed on polyolefins.
Real-world plastic waste adds its own difficulty. Environmental microplastics
are not pure polymers; they are mixtures of polymer types, each with its own
additives, weathering, surface contamination by organic matter and inorganic
particles, and colonisation history. Enzymes tuned for pure amorphous PET
may stumble on weathered, coloured, additive-laden post-consumer PET, and
enzymes that perform in controlled conditions may be inhibited or quickly
inactivated in messy environmental matrices. Testing under realistic
conditions, in soils, sediments, and natural waters, is often missing from the
literature.
At the engineering level, moving from bench to environmental remediation or
industrial bioprocessing is far from trivial. Enzyme production costs are still
high, though expression systems in industrial hosts (Bacillus subtilis,
Corynebacterium glutamicum, Pichia pastoris) and better fermentation
economics are slowly bringing them down. Designing reactors for solid-liquid
reactions with heterogeneous plastic substrates calls for solutions quite
different from those used with soluble substrates.
Economics run through all of it. In today’s market, mechanically recycled
plastic is cheaper to make than enzymatically depolymerised and biologically
valorised plastic. The case for biological recycling rests on the value of what
comes out (TPA, EG, PHAs, platform chemicals), the cost of producing enzymes
and running the process, and above all the policy setting, particularly carbon
pricing, extended producer responsibility, and recycled-content standards.
9
Without real carbon pricing or recycled-content mandates, the incentive to
invest stays weak.
Finally, releasing plastic-degrading microorganisms or engineered enzymes
into the environment carries ecological risk that needs careful evaluation.
Putting genetically modified organisms with improved degrading ability into
open systems raises containment and biosafety questions. Even wild-type
degraders, if introduced where they were not already resident, could affect
native microbial communities, nutrient cycling, and ecosystem function in ways
no one intended.
8. Future Directions
The field sits at a turning point. The foundational science is mature enough to
point to the most promising biological systems, yet a wide gap still separates
laboratory discovery from real-world use. A few research directions look likely
to define the next decade.
Multi-omic discovery of new enzymes is probably the most immediately useful
avenue. Environmental metagenomics has already grown the catalogue of
polyester hydrolases from a handful of characterised enzymes to thousands of
candidate sequences in global databases such as PlasticDB and dbCAN.
Metatranscriptomics and metaproteomics can show which of those genes are
actually expressed in plastisphere communities, narrowing the list for
functional testing. Machine-learning models trained on the growing pool of
enzyme sequence-function data can predict activity from sequence alone,
which makes it possible to screen millions of environmental sequences
virtually. This pairing of metagenomic mining with AI should turn up enzymes
that complement existing tools, especially for the tough polyolefins.
Synthetic biology could let researchers engineer microbial chassis that perform
complete degradation and valorisation in one organism. By assembling
enzymatic modules, a surface-active oxidative enzyme to start the attack, an
alkane hydroxylase to shorten chains, and a β-oxidation pathway for full
mineralisation or diversion into PHA biosynthesis, in a robust chassis such as
Pseudomonas putida KT2440 (which tolerates toxic aromatics), one could build
plastic-eating cell factories that grow on specific polymers as their sole carbon
source. Cell-free systems, where purified enzyme cocktails act on plastic
without living cells, offer an alternative with advantages in containment,
reproducibility, and process control.
Materials-science pre-treatment could speed degradation dramatically.
Mechanochemistry (ball milling), supercritical fluid treatment, ionic liquid
dissolution, and plasma surface activation all raise surface area, lower
10
crystallinity, and add functional groups that make the polymer easier for
enzymes to reach, and they do so without the environmental downsides of
chemical oxidants. Combining such pre-treatments with optimised enzyme
cocktails in closed-loop bioreactors is a realistic near-term path to economically
viable enzymatic recycling at industrial scale.
In situ bioremediation of contaminated soils, sediments, and water bodies
needs a different playbook from industrial bioprocessing. Bioaugmentation
(introducing specialised degrading strains) and biostimulation (adding
nutrients to spur native degraders) are established in hydrocarbon cleanup and
could be adapted for microplastics. Phytoremediation of contaminated soils
using plants that recruit plastic-degrading rhizobacteria is another idea worth
pursuing. Self-amplifying biofilm systems, in which plastic-degrading bacteria
are encapsulated in slow-release formulations that build persistent
communities on plastic surfaces, could keep remediation going over months to
years.
Policy and regulation will matter as much as the technology. The Plastics
Treaty now under negotiation at UNEP, extended producer responsibility rules
in the EU and UK, and recycled-content mandates for packaging all create
market signals that reward investment in new recycling technologies. Stronger
carbon markets could add revenue streams for plastic valorisation. Engaging
with these processes, so that enzymatic recycling is recognised and rewarded
appropriately, is a legitimate and important task for the scientific community.
9. Conclusion
This review has drawn together the current state of knowledge on the
microbial enzymatic degradation of microplastics, from the ecology of the
plastisphere through the molecular mechanisms of the main degrading
enzymes to the applied goal of a circular bioeconomy where plastic waste
becomes high-value products.
The overall picture is one of cautious optimism. The evidence is clear that
microorganisms have evolved, partly in response to the plastic pollution of
recent decades, a capable set of enzymatic tools for attacking synthetic
polymers. For PET, the PETase–MHETase system of Ideonella sakaiensis and
the thermostable cutinase variants built from it are real advances: they enable
complete depolymerisation to recyclable monomers at conditions close to
industrial viability. Upcycling PET-derived TPA and EG into high-value
bioproducts gives both an economic and an environmental reason to invest in
enzymatic recycling.
11
For the polyolefins, PE, PP, PS, and PVC, the task is far harder, and the field is
earlier in its development. Oxidative enzymes (laccases, peroxidases,
oxygenases) can start the degradation but are slow, non-specific, and difficult
to engineer for the solid-liquid interface where they have to work. Progress
here will likely depend on multi-omic discovery of new enzymes, computational
design of better variants, and combined abiotic-biotic strategies in which pre-
treatment leaves a more vulnerable polymer surface for enzymes to finish.
The plastisphere is both a natural model for studying plastic biodegradation
and a reservoir of new degrading microorganisms and enzymes for
biotechnology. Metagenomics, metatranscriptomics, and metaproteomics are
expanding what we know about its functional ecology quickly, though the gap
between detecting a gene and confirming what it does in practice remains a
persistent challenge.
An honest conclusion has to admit that enzymatic degradation alone will not
solve the microplastic crisis. At environmental concentrations and under real
conditions, degradation is too slow to stop plastic waste from accumulating.
Enzymatic approaches have to sit within a broader strategy: sharp cuts in
plastic production, an end to single-use plastics, investment in collection and
sorting, and genuinely biodegradable replacement materials. Even so, for the
vast quantity of plastic already in the environment and the waste stream,
enzymatic degradation and valorisation is the most promising way to close the
plastic carbon cycle in a way that works environmentally and economically.
In short, microbial enzymatic degradation of microplastics, from the
ecophysiology of the plastisphere through the enzymology of the catalysts to
the bioeconomy of monomer valorisation, is one of the most practically urgent
frontiers in modern biotechnology. The next decade of research, guided by
multi-omic discovery, computational protein design, and synthetic biology, will
decide whether this biological potential becomes the remediation our planet
needs.
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