The present invention relates to a foamed plastic composition comprising at least one polymer and at least one active agent, wherein said foamed plastic composition is at least partially coated with the active agent.

Nanoscopic dispersion of trace enzymes and random heteropolymers in plastics provides to fully functional plastics with eco-friendly microplastic elimination and programmable degradation.

Compositions comprise synergistic enzyme mixtures, and related methods, to realize near-complete depolymerization in biodegradable polymer/additive blends.

The invention relates to treatment of waste with one or more microorganisms for the purposes of, including but not limited to, degrading waste, bioremediation of waste, enhancing waste stabilization, reducing contaminants in waste, reducing odor in waste, reducing organics in waste, and combinations thereof. More particularly, the invention relates to isolated Bacillus strains, and strains having all of the identifying characteristics of these strains, and combinations thereof, for uses comprising the above-mentioned uses.

The present invention includes methods for preparing anticoagulant polysaccharides using several non-naturally occurring, engineered sulfotransferase enzymes that are designed to react with aryl sulfate compounds instead of the natural substrate, PAPS, to facilitate sulfo group transfer to polysaccharide sulfo group acceptors. Suitable aryl sulfate compounds include, but are not limited to, p-nitrophenyl sulfate or 4-nitrocatechol sulfate. Anticoagulant polysaccharides produced by methods of the present invention comprise N-, 3-O-, 6-O-sulfated glucosamine residues and 2-O sulfated hexuronic acid residues, have comparable anticoagulant activity compared to commercially-available anticoagulant polysaccharides, and can be utilized to form truncated anticoagulant polysaccharides having a reduced molecular weight.

The present invention relates to a process of enzymatic degradation of an absorbent structure, the absorbent structure being suitable for providing an absorbent core of a hygiene article, wherein the process comprises the step of contacting the absorbent structure with a solution comprising enzymes; wherein the absorbent structure comprises a polysaccharide superabsorbent polymer, such as a cellulose-based or a starch-based superabsorbent polymer.

Provided are an enzyme complex for decomposing polyethylene terephthalate (PET), a method for decomposing waste plastic using the enzyme complex, and a manufacturing method of the enzyme complex. According to the present disclosure, since the enzyme complex is a complex form of Ideonella sakaiensis-derived PETase and Candida Antarctica-derived lipase (CALB) by dockerin-cohesin binding and is simultaneously applicable to a substrate to be decomposed, it is possible to exhibit a synergistic effect on the decomposition of polyethylene terephthalate. In addition, it is possible to provide a stable enzyme complex of decomposing polyethylene terephthalate by providing a mini-scaffolding protein obtained by miniaturizing cellulosome as a scaffolding protein. In particular, the mini-scaffolding protein includes an A-type CBM3 module as a carbohydrate binding module to increase the accessibility to polyethylene terephthalate, a substrate to be decomposed, and to have quickly and efficiently polyethylene terephthalate decomposition activity.

Novel ways of degrading polyamides including Nylon 6 and Nylon 6,6 (polycaprolactam) are disclosed. Microorganisms originally sourced from the environment are utilized to produce an enzyme(s) useful for degrading polyamides. can be degraded by a cutinase, a lipase, or a combination thereof.

Industrial fermentation for the production of lactic acid from organic waste combined with chemical recycling of polylactic acid are provided, to obtain lactic acid at high yields.

The present disclosure relates to a non-naturally occurring enzyme that includes a first polypeptide that catalyzes the hydrolysis of a polyester to produce mono-(2-hydroxyethyl) terephthalate (MHET), a second polypeptide that catalyzes the cleavage of MHET to produce at least one of terephthalic acid or ethylene glycol, and a third polypeptide that links the first polypeptide with the second polypeptide.