Knowledge about extremophile organisms and their survival strategies could be of great value for various industrial applications including biological plastics recycling. The black fungus Knufia chersonesos inhabits extreme environments such as rocks and therefore produces specific enzymes that function under harsh conditions. A cutinase (Kc_Cut) and a lipase (Kc_Lip) identified via proteomics-based screening in the secretome of K. chersonesos grown on poly (butylene-adipate-co-terephthalate) (PBAT) as carbon sources were recombinantly expressed in Komagataella phaffii and Trichoderma reesei, respectively, for further characterization. The purified enzymes showed a specific activity of 83 ± 1 and 0.23 ± 0.02 U mg-1 on para-nitrophenylbutyrate (p-NPB) as substrate, respectively. Optimum conditions of Kc_Cut were evaluated through activity measurements on p-NPB and resulted in 50 °C, pH 8 and 100 mM potassium phosphate buffer. Incubation with PBAT powder for 72 h resulted in the release of 17 ± 1 µM of terephthalic acid (Ta) by Kc_Cut while the Kc_Lip liberated the trimer BTaB. This indicated a cooperative action of the two enzymes which was confirmed by hydrolysis of BTaB by Kc_Cut and provides valuable insight into the metabolic potential and adaptability of K. chersonesos.

Regenerated cellulosic fibers, such as lyocell fibers, are fully biodegradable and of 100

Sulfuric acid is one of the most widely used industrial chemicals, yet its conventional production depends on purified sulfur, chemical catalysts, and energy-intensive processes. In contrast, sulfur-oxidizing bacteria can convert reduced inorganic sulfur compounds into sulfuric acid under mild conditions. To optimize biological sulfuric acid production, six Acidithiobacillus thiooxidans strains were first studied on chemical sulfur, with strain DSM 14887 showing the highest sulfur-oxidation activity. This strain, along with intermediate- and low-performing strains, were then investigated on biogas-derived sulfur collected from a digester and external desulfurization units. Remarkably, sulfate production from 1% biogas-derived sulfur reached 0.34 M, 2.5-fold increase compared to chemical sulfur. Increasing the biogas-derived sulfur load to 6% further improved performance, yielding 0.80 M sulfate, a seven-fold increase compared to chemical sulfur. Ultimately, the prolonged incubation led to the complete oxidation of the 6% sulfur, yielding 2 M sulfate. The characterization of the biogas-derived sulfur using scanning electron microscope, water contact angle measurements, and ATR-FTIR revealed several features that explain its enhanced reactivity. The material displayed a more heterogeneous particle size distribution and a more hydrophilic surface, as indicated by a lower contact angle (73 ± 2°) compared to chemical sulfur (100 ± 5°). FT-IR spectra also showed functional groups associated with proteins and polysaccharides. Together, these properties make biogas-derived sulfur a particularly effective substrate for microbial sulfuric acid production and a promising alternative to conventional acid-production processes.

Water-soluble polymers have exceptional properties and are therefore used in many applications. Many of these products end up down the drain; therefore biodegradability, especially in wastewater treatment plants, is essential to prevent accumulation in the environment. This study examined recombinant hydrolases PahZ1KT-1 and PahZ2KT-1 from Sphingomonas sp. KT-1 and PahZ1KP-2 from Pedobacter sp. KP-2 for their role in biodegrading water-soluble poly(aspartic acid) (tPAA). Analysis by a turbidity assay and Gel Permeation Chromatography (GPC) revealed highest activity of PahZ1KT-1 and PahZ1KP-2 at pH 8 and 40 °C on tPAA, whereas PahZ2KT-1 showed no activity on the polymer but yet on its oligopeptides with highest values at pH 7 and 55 °C. GPC analysis revealed that PahZ1KT-1 and PahZ1KP-2 hydrolyzed tPAA (MN > 17,000 Da) into oligopeptides (>500 Da), while PahZ2KT-1 further degraded them to α-di(l-aspartic acid) and l-aspartic acid. Combined, these enzymes synergistically decomposed tPAA completely into l-aspartic acid within 24 h. Supplementation of hydrolases into standardized biodegradation test improved biodegradation (54 %) of tPAA after 28 d. Supplementing PahZ1KT-1 or PahZ1KP-2 alone achieved 52 % and 54 % tPAA biodegradation, respectively. Preincubating tPAA with hydrolases boosted degradation to 71 % in 28 d. These findings highlight enzymes' crucial role in breaking down macromolecules into lower molecular weight species for effective tPAA biodegradation.

Cutinase from Thermobifida cellulosilytica was site specifically conjugated with aromatic tether containing TA4C at the N-terminus. Both phenylpropyl-TA4C and naphthyl-TA4C conjugated cutinase (PP-Cut and NP-Cut) release more than two times higher terephthalic acid than unconjugated cutinase after 24 h. The aromatic tether conjugated cutinases also exhibits higher hydrolysis activity against less degradable PET fabrics. Scanning electron microscopy confirmed that conjugated variants show extensive surface erosion which is accelerated by enhanced enzyme-polymer interactions.

Plastic waste as a permanent pollutant in the environment is of increasing concern due to its largely unknown long-term effects on biota. The occurrence in rivers, has, compared to research in the oceans, only become the focus of scientific investigations in the last few years. The Austrian Alps in particular are largely unexplored in this respect. Therefore, the Alplast project addresses microplastic transport from the glaciers at the summit over steep mountain torrents to the lowland rivers and aims in conducting a first inventory of the alpine area. Specifically, analyses of microplastic occurrences are being carried out from the Sonnblick glacier via the Rauriser Ache, the Salzach, the Inn and the Danube and are intended to expand the understanding of processes with regard to the behaviour of microplastics in the water cycle from the glacier to the valley. The influence of snowmelt as well as the temporal development, which can be determined from ice cores, are of great interest. In addition, questions regarding the origin and distribution of plastic in flowing waters as well as the possible biological degradation by microorganisms will be clarified.Since the sampling areas cover entire catchments at different altitudes, different methodologies and devices are used. For the studies on the glaciers, the snow cover as well as ice cores are sampled and analysed. In the rivers a multi-point method is used due to the spatial distribution of plastic particles in the river cross-section. But the net samples at different depths are combined with isokinetic pump sampling in order to detect the widest possible size range. Isokinetically taken pump samples have the great advantage that a weighting process takes place directly during sampling. This means that samples can be taken in different areas (high and low flow velocities) of the cross-section (together with the nets) and then a composite sample can be analysed for the profile. Particle counts, classification and the measurement of concentrations and loads are then used to determine quantities and the most common types of plastics in the alpine environment. The measuring stations were selected in such a way that more and more potential microplastic sources are added in the course of the catchment in order to achieve the best possible process understanding regarding the origin and fate of the plastic waste.

Electronic waste is a valuable source of critical metals like nickel and cobalt, but their recovery is challenging. Current recycling processes use harsh conditions and toxic chemicals, which is why environmentally friendly alternatives are crucial. Metal-binding peptides offer high selectivity and durability, making them promising for sustainable metal separation. Here, phage display was successfully applied to screen a combinatorial peptide library with specific affinities to nickel or cobalt. Identified peptides with the amino acid sequences FWPLHHH, GPHKHHA, HNYHHRH, and HMNHHHH revealed improved binding affinities of up to 20.000-fold to immobilized metal ions compared to the unspecific binding of the phage backbone. Furthermore, low micromolar dissociation constants e.g., 6.2 µM for peptide Co_02 (HMNHHHH) to Co2+ and 29.0 µM for peptide Ni_01 (GPHKHHA) to Ni2+, determined by Isothermal Titration Calorimetry (ITC) measurements confirmed the intrinsic metal binding properties. These peptides offer a high potential for future recycling of nickel and cobalt from mixed metal waste like batteries.

The potential of three thermophilic enzymes from the alpha,beta-hydrolases superfamily, that have recently been described for polyester hydrolysis, was investigated for polyester synthesis, esterification and transesterification reactions. The hydrolases (LCC, leaf-branch compost cutinase; its variant LCCICCG, Thb from Thermoanaerobacterales bacterium) were recombinantly expressed, purified and immobilized onto polypropylene beads. A design of experiments (DoE) assisted study was performed to investigate their synthetic potential to produce short flavor esters by analyzing their thermostability and selectivity towards alcohols and acids with different chain lengths. The factors considered in the DoE (i.e., temperature, alcohol chain length, acid chain length and reaction time) were optimized using MODDE (R) software to generate a predictive model defining the optimal synthetic conditions for the three enzymes. In each experiment, the monitored response was the acid conversion rate, quantified with GC-FID analysis. For synthesis, the temperature optima of LCC, LCCICCG and Thb were 60 degrees C, 55 degrees C, and 80 degrees C, respectively, corresponding to the maximum percentage of monomers conversion for long-chain alcohols and acids as substrates. Polymerization of dimethyl adipate and 1,8-octanediol as building blocks was carried out to confirm the applicability of the obtained model for the synthesis of larger macromolecules via polycondensation reactions. The proposed approach highlights the innovative application of these novel thermophilic enzymes, traditionally associated with hydrolytic functions, as effective biocatalysts in synthetic processes, enabling the production of a well-known class of polyesters through an alternative and sustainable enzymatic route. Conversion of monomers, as determined by nuclear magnetic resonance (NMR) analysis, was similar to 90 % for all enzymes while the average molecular weights (M-n) of the polyesters, analyzed by gel permeation chromatography, were between 3600 Da, for LCC and its variant LCCICCG, and 3800 Da for Thb.

Casein-based materials offer a sustainable platform for advanced biomaterials, yet the impact of ionic strength on their macroscopic structure and properties remains largely unexplored. This study investigates the coagulation (and gelation) of sodium caseinate solutions (14-20 wt%) at the isoelectric point in citric acid-trisodium citrate buffers of varying strengths (30-300 mM). The results demonstrate that buffer strength significantly influences water content, compactness, mechanical strength, and optical properties of the formed hydrogels. Notably, samples coagulated in 100 mM buffer exhibited lower compactness and tensile strength, and greater opacity compared to those formed in 300 mM buffer. Treatment with glycerol, which also induces partial dehydration, proved valuable in preventing structural collapse during drying, enabling structural insights through scanning electron microscopy. Additionally, glycerol played a crucial role in enhancing the samples' rehydration capability. The study also revealed a hydroresponsive switchable opacity, a feature that could be leveraged for applications such as wound dressings that indicate exudate saturation. Furthermore, the ability to tune the mechanical properties and structural compactness could be useful for designing tissue engineering scaffolds and drug delivery carriers. These findings provide critical insights into tailoring casein-based biomaterials through controlled coagulation conditions.

This study investigates enzymatic hydrolysis of four novel polyesters (REPolymers) with different structures based on terephthalic acid, ethylene glycol, glutaric acid, and decanediol. These polyesters were synthesized from PET building blocks and bio-based monomers. A hydrolase from Rhizobacter sp. (Rhb), identified from a wastewater treatment sludge metagenome, was used to predict biodegradation and to assess enzymatic recycling potential of the REPolymers. Rhb shows homology to Ideonella sakaiensis PETase but exhibits superior thermostability and activity due to specific amino acids previously identified in PETase engineering. Using mass spectrometry and HPLC-DAD analysis, hydrolysis of REPolymers (5 - 34 kDa) was mechanistically studied. Mono-(2-hydroxyethyl) terephthalic acid (MHET) was the primary product, with longer PET oligomers and aliphatic dimers also detected, indicating endo-wise cleavage of aromatic and aliphatic ester bonds. Consistent degradation patterns showed dimer accumulation across different REPolymers. These findings illuminate how the polyester structure affects enzymatic hydrolysis, supporting the development of novel waste/bio-based polymers and recycling strategies.

Despite recent advances, there is still a demand for more efficient enzymes hydrolyzing synthetic polymers. Automated high throughput screening strategies of microorganisms from different environments could yield novel enzymes but require specific methods for detection of polymer hydrolysis in complex matrices. Here, 5-carboxy-fluorescein (5-FAM) was covalently coupled to poly(butylene adipate) (PBA) and blended at 1 %, 5 % and 10 % w/w concentrations with non-labeled PBA. Hydrolysis of PBA by the Thc_Cut1 cutinase from Thermobifida cellulosilytica was confirmed via quantification of the released monomers 1,4-butanediol and adipic acid, weight loss and FTIR analysis. Upon incubation with Thc_Cut1, hydrolysis of all three fluorescent labeled PBA blends lead to a clear fluorescence increase of up to 4000 RFU while no signal change was detected for the blank and for heat-inactivated enzyme (signal below 500 RFU). In a next step, as a model organism Pichia pastoris expressing the identical cutinase was cultivated in the presences of labeled PBA. Despite the complex matrix, a fluorescence increase of up to 500 RFU was observed for P. pastoris expressing the enzyme while no significant signal change was seen for the control strain (lacking Thc_Cut1 expression). Likewise, extracellular enzymes from the fungi Fusarium solani and Alternaria alternata hydrolyzed labeled PBA leading to fluorescence increases of 1328 and 1187 RFU. This indicates that 5-FAM covalently coupled to polymers could be used for development of simple and high throughput screening platforms to identify polymer decomposing microorganisms and enzymes.

This study focuses on the biochemical characterization of a new hydrolase (Thb) expressed from anaerobic Thermoanaerobacterales, which could be used to improve biogas plant efficiency for plastic waste treatment. The specificity of Thb for various polyesters, including polyethylene terephthalate (PET), polybutylene adipate terephthalate (PBAT), polybutylene succinate (PBS), and polylactic acid (PLA), was compared to the well-studied cutinase HiC from Humicola insolens. Based on gravimetric analysis and quantification (high-performance liquid chromatography (HPLC)) of monomers solubilized upon enzymatic hydrolysis, Thb was found to be more active on aromatic polyesters, while HiC led to a higher amount of hydrolysis products on aliphatic polyesters (PBS and PLA). Polyester hydrolysis was further investigated by scanning electron microscopy and infrared spectroscopy. A comparison of the two enzyme structures indicated the higher aromatic character of specific regions of the Thb surface as a possible reason for these differences in specificity.

Lipophilic wood extractives (LWEs), including triterpenes, fatty acids, resin acids, waxes, alcohols, sterols, sterol esters, and glycerides, pose significant challenges for pulp and paper mills. Microbial triacylglycerol lipases (EC 3.1.1.3), stable at high temperatures and pH, offer a solution by hydrolyzing detrimental triglycerides into free fatty acids, which can be solubilized in alkaline environments. However, inconsistent performance and limited understanding of process dynamics under industrial conditions have hindered their application. This study evaluated the effects of phenols, salts, and organic acids on lipase activity using a p-nitrophenyl butyrate assay. Additionally, the influence of pulp and process waters was assessed using a self-established assay designed to mimic process conditions and analyze complex matrices. Among five tested microbial lipases, those from Burkholderia cepacia and Thermomyces lanuginosus exhibited up to a 220 % increase in activity at 150 mM sodium-sulfate, as well as enhanced activity with higher acetate concentrations. In contrast lipases from Candida rugosa, Candida antarctica, and Rhizopus oryzae did not respond to kosmotropic ions (Mg2+ and SO42-). Most lipases benefitted from lignin-derived phenolic compounds containing syringol moieties. Notably, lipase from Burkholderia cepacia exhibited a 230 % activity increase with 1 mM syringic alcohol. Conversely, linoleic acid above its critical micelle concentration and abietic acid inhibited all enzymes except the lipase from Candida rugosa. Magnesium ions mitigated linoleic acid's inhibitory effect through charge neutralization, enabling maximum activity. The addition of 10 mM Mg2+ ions decreased the zeta potential of a lipid emulsion composed of triolein and linoleic acid from -55 mV to -10 mV, and increased triglyceride conversion with Thermomyces lanuginosus lipase from 0 to -72 %. This study identifies key factors influencing enzymatic hydrolysis of triglycerides and elucidates interactions with compounds common in pulp mills, advancing the development of efficient enzymatic treatments.

The environmental challenges presented by plastic waste, particularly poly(ethylene terephthalate) (PET), necessitate innovative biodegradation strategies. The cutinase from Thermobifida cellulosilytica, Thc_Cut1 (Cut), was site-specifically conjugated with alkyl tethers of varying lengths (C3, C6, C9) through 1H-1,2,3-triazole-4-carbaldehyde (TA4C) derivatives. These conjugations were designed to enhance affinity for PET by adjusting the enzyme's hydrophobicity. The enzyme kinetic parameters of both conjugated and unconjugated cutinases revealed that the modifications have a minimal impact on catalytic activity. However, a significant improvement in the PET hydrolysis efficiency was observed. Specifically, hexyl and nonyl TA4C-containing cutinase displayed notable increases in terephthalic acid (TPA) release, exceeding the performance of unconjugated cutinase by 65% and 69%, respectively. Scanning electron microscopy and water contact angle measurements confirmed the enhanced erosion and hydrophilicity of the PET surface following the enzyme treatment. Increased enzyme adsorption on the PET surface for C6-Cut and C9-Cut was validated by X-ray photoelectron spectroscopy. Moreover, high-speed atomic force microscopy demonstrated faster and more stable adsorption of C6-Cut and C9-Cut on PET surfaces compared with the slower adsorption of unconjugated cutinase. Additionally, molecular dynamics simulations indicate a higher affinity of conjugated cutinase for PET film. These results suggest that conjugating an alkyl tether to the N-terminus strengthens the interaction between cutinase and PET, improving hydrolysis.

The growing issue of petroleum-based polymer waste demands sustainable recycling strategies, with enzymatic processes offering a promising solution. This study investigates enzymatic decomposition of polyethylene terephthalate (PET) and polybutylene adipate terephthalate (PBAT) by Gordonia species, known for their pollutant-degrading capabilities. When cultivated with PET, G. phthalatica, G. paraffinivorans, and G. alkanivorans showed esterase activity on para-nitrophenyl butyrate (pNPB). G. phthalatica reached highest activity (485.0 ± 34.0 mU mL-1) and released 9.2 ± 0.6 μM terephthalic acid (TPA) from PET. Sequence alignment revealed three cutinases for polyester hydrolysis (Gph_Cut1, Gpa_Cut1, Gpa_Cut2) which were expressed in E. coli. The enzymes were active at pH 6 and ≥ 45 °C and retained up to 70 % of their activity after 96 h at 30 °C. The cutinases hydrolyzed PBAT, releasing up to 47.0 ± 1.5 μM TPA. In contrast, PET hydrolysis yielded soluble oligomers hydrolyzable to 57.6 ± 0.1 μM TPA using a commercial cutinase. The data show that Gordonia species could contribute to the biodegradation of PBAT in nature.

Some wounds do not follow the typical healing trajectory and show very little, if any, progress. They dreadfully threaten the patients' quality of life and may even lead to limb amputation and death. Several interrelated systemic and local factors may cause a delay in wound healing. The microenvironment of these wounds can be different from wounds that heal spontaneously or with standard treatment. As discussed in the present work, proteases' levels or activity can be elevated in some cases of chronic ulcers; infection can aggravate the situation. A detailed overview of the proteases' effect on wound healing is presented in this work. Assuming untimely or irregularly excessive proteolytic activity plays a pathological role, some researchers targeted attenuation of protease level as a strategy to promote healing. This can be done via different approaches, including physical removal, inhibiting their activity, and controlling their expression directly through gene silencing or indirectly, for instance, by resolving infection. Apart from targeting protease modulation as a therapeutic strategy, many studies have examined the protease state to gain insights into the underlying mechanisms by which a remedy, dressing, or specific therapy has affected the healing process. This study aims to provide an overview of the studies in these two categories. Of course, various proteases are involved in the healing process, but in each study, usually, only one or some of them are investigated; matrix metalloproteinase-2 (MMP-2), MMP-9, and human neutrophil elastase (HNE) are among them. Furthermore, in some cases, cumulative proteolytic activity is evaluated in terms of gelatinolytic, collagenolytic, or caseinolytic activity, which is also absolutely beneficial. Some research groups have considered the potential of proteases as a diagnostic or prognostic biomarker and have tried to develop some sensors or indicators; this topic is also covered in the present work. To control protease activity, researchers have employed strategies such as introducing groups with negative charges to cellulosic dressings for better interaction with positively charged protease, inhibiting matrix metalloproteinases (MMPs) by chelating metal ion cofactors, silencing MMPs gens via small interfering ribonucleic acid (siRNA) that releases from nanocarriers, and using superabsorbent dressings to absorb proteases. image

The study demonstrates the potential of enzymatic hydrolysis and alkaline pretreatment for sustainable blended textile recycling. The target is complete cellulose removal while preserving the polyester integrity for recovery. Interactions of sodium hydroxide concentration (10 %-30 %), urea concentration (0 %-12 %), and temperature (-20 degrees C-50 degrees C) were investigated during pretreatment using a design of experiments. Analysis revealed a bimodal pattern in polyester mass loss, with one peak at lower concentrations and temperatures, and a more prominent peak at higher concentrations and temperatures. Cellulose hydrolysis also occurred under high NaOH concentrations and elevated temperatures (50 degrees C, 30 % NaOH, 0 % urea). Optimal conditions, preserving polyester integrity while achieving complete cellulose elimination, were identified at temperatures between 6.2 degrees C and 13.3 degrees C, with NaOH concentrations of 20.7 %-26.6 % (0 % urea) or 13.9 % NaOH and 12 % urea. These findings pave the way for a greener, more efficient textile recycling, advancing the circularity for textiles.

A variety of important agricultural crops host fungi from the Aspergillus genus can produce cancerogenic secondary metabolites such as aflatoxins. Consequently, novel strategies for detoxification and their removal from food and feed chains are required. Here, detoxification of Aflatoxin B1 (AFB1) by the Bacillus subtilis multi-copper oxidase CotA (BsCotA) was investigated. This laccase was recombinantly produced in E. coli while codon optimization led to duplication of the amount of active protein obtained. CuCl2 was added to the cultivation medium leading to a 25-fold increase of Vmax corresponding to improved incorporation of Cu2+ into the enzyme protein which is essential for the catalytic reaction. To avoid potential cytotoxicity of Cu2+, cultivation was performed at microaerobic conditions indeed leading to 100x more functional protein when compared to standard aerobic conditions. This was indicated by an increase of Vmax from 0.30 ± 0.02 to 33.56 ± 2.02 U/mg. Degradation kinetics of AFB1 using HPLC with fluorescence detection (HPLC-FLD) analysis indicated a theoretical substrate saturation above solubility in water. At a relatively high concentration of 500 μg/L, AFB1 was decomposed at 10.75 μg/Lh (0.17 nmol*min−1*mg−1) at a dosage of 0.2 μM BsCotA. AFQ1 and epi-AFQ1 were identified as the initial oxidation products according to mass spectrometry (i.e., HPLC-MS, HPLC-QTOF). None of these molecules were substrates for laccase but both decomposed in buffer. However, decomposition does not seem to be due to hydration of the vinyl ether in the terminal furan ring. Genotoxicity of the formed AFB1 was assessed in several dilutions based on the de-repression of the bacterial SOS response to DNA damage indicating about 80-times reduction in toxicity when compared to AFQ1. The results of this study indicate that BsCotA has high potential for the biological detoxification of aflatoxin B1.

Every 1.2 s, a diabetic foot ulcer is developed, and every 20 s, one amputation is carried out in diabetic patients. Monitoring and controlling protease activity have been considered as a strategy for more efficient management of diabetic and other chronic wounds. This study aimed to develop a casein-based dressing that, by its disappearance, provides information about the activity of proteases and simultaneously harnesses proteolytic activity. Casein films were fabricated by using an aqueous solution, and heat treatment was successfully deployed as a green and clean approach to confer hydrolytic stability. Our results showed that casein-based films' mechanical characteristics, water absorption, and proteolytic stability could be controlled by the length of the heat treatment, which proved to be a useful tool. An increase in the treatment duration from 30 min to 3 h led to toleration of 2.4 times higher stress, 2 times lower water uptake, and 3.4 times higher proteolytic stability at examined conditions. Selected casein-based structures responded to Bacillus sp. bacteria's protease (BSP) and human neutrophil elastase (HNE) as representatives of bacterial and nonbacterial proteases found in the wounds at 10 and 200 ng mL(-1) levels, respectively. The hydrolysis was accompanied by a 36% reduction in proteolytic activity measured by using a casein-based universal protease activity assay. The released casein fragments could scavenge 90% of the examined radicals. In-vitro cell culture studies showed that the hydrolysates were not cytotoxic, and the casein-based film had a favorable interaction with fibroblast cells, indicating its potential as a scaffold in the case that proteolytic activity would not be to the extent that causes its rapid disintegration. In general, these findings hold promise for applying the developed casein-based structure for detecting proteolytic activity without the need for any equipment, kits, or expertise and, more importantly, in a highly economical manner. In the case that the proteolytic activity would not be severe, it could also serve as a substrate for cell adhesion and growth; this would aid in the healing process.

The urge to discover and develop new technologies for closing the plastic carbon cycle is motivating industries, governments, and academia to work closely together to find suitable solutions in a timely manner. In this review article, a combination of uprising breakthrough technologies is presented highlighting their potential and complementarity to be integrated one with the other, therefore providing a potential solution to efficiently solve the plastics problem. First, modern approaches for bio-exploration and engineering of polymer-active enzymes are presented to degrade polymers into valuable building blocks. Special focus is placed on the recovery of components from multilayered materials since these complex materials can only be recycled insufficiently or not at all by existing technologies. Then, the potential of microbes and enzymes for resynthesis of polymers and reuse of building blocks is summarized and discussed. Finally, examples for improvement of the bio-based content and enzymatic degradability and future perspectives are given.