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The demand for environmentally friendly products allied with the depletion of natural resources has increased the search for sustainable materials in chemical and pharmaceutical industries. Polyesters are among the most widely used biodegradable polymers in biomedical applications. In this work, aliphatic polyesters (from globalide and ω-pentadecalactone) were synthesized using a new commercial biocatalyst, the low-cost immobilized NS 88011 lipase (lipase B from Candida antarctica immobilized on a hydrophobic support). Results were compared with those obtained under the same conditions using a traditional, but more expensive, commercial biocatalyst, Novozym 435 (lipase B from C. antarctica immobilized on Lewatit VP OC). When NS 88011 was used in the polymerization of globalide, longer reaction times (240 min)-when compared to Novozym 435-were required to obtain high yields (80-90 wt%). However, higher molecular weights were achieved. When poly(ω-pentadecalactone) was synthesized, high yields and molecular weights (130,000 g mol-1) were obtained and the enzyme concentration showed strong influence on the polyester properties. This is the first report describing NS 88011 in polymer synthesis. The use of this cheaper enzymatic preparation can provide an alternative for polyester synthesis via enzymatic ring-opening polymerization.

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The facile preparation of poly(l-DOPA)-tyrosinase (PDM-Tyr) composite and its application both in substrate (phenol) and inhibitor (atrazine) sensing is reported here for the first time. Effective immobilization of enzyme is realized via in-situ entrapping Tyr in poly(l-DOPA) (PDM), which is formed by Tyr catalytic polymerization of l-DOPA. The Tyr modified electrode is simply prepared by dipping the PDM-Tyr composite on an Au electrode and then covered by Nafion. The thus-prepared Tyr-immobilized electrode exhibits excellent performance superior to most Tyr-based electrochemical biosensors, the sensitivity to phenol is as high as 5122 µA mM(-1) in the linear range of 10nM~1.25 µM, the apparent Michaelis-Menten constant (KM(app)) determined as low as 3.13µM indicates strong substrate binding and high catalytic activity of the immobilized Tyr. The biosensor also works well in atrazine biosensing, with a linear detection range of 50ppb~30ppm and a low detection limit of 10ppb obtained. In addition, the biosensor shows excellent stability, precision, high sensitivity and fabrication simplicity.

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An environmentally friendly water-soluble conjugated polythiophene poly[2-(3-thienyl)-ethoxy-4-butylsulfonate] (PTEBS) has been found to be effective for making hybrid solar cells. In this work, we first report the enzyme-catalyzed polymerization of (3-thienyl)-ethoxy-4-butylsulfonate (TEBS) using horseradish peroxidase (HRP) enzyme as a catalyst and hydrogen peroxide (H2O2) as an oxidant in an aqueous buffer. This enzyme-catalyzed polymerization is a "green synthesis process" for the synthesis of water-soluble conjugated PTEBS, the benefits of which include a simple setting, high yields, and an environmentally friendly route. Fourier transform infrared spectra (FTIR) and UV⁻Vis absorption spectra confirm the successful enzyme-catalyzed polymerization of TEBS. The thermo gravimetric (TG) data show the obtained PTEBS is stable over a fairly high range of temperatures. The present PTEBS has a good solubility in water and ethanol, and photoluminescence quenching of PTEBS/titanium dioxide (TiO2) composite implies that the excitons dissociate and separate successfully at the interface of PTEBS and TiO2, which help to build solar cells using green processing methods.

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Thermally synthesized poly(aspartic acid) (tPAA) is a bio-based, biocompatible, biodegradable, and water-soluble polymer that has a high proportion of ß-Asp units and equivalent moles of D- and L-Asp units. Poly(aspartic acid) (PAA) hydrolase-1 and hydrolase-2 are tPAA biodegradation enzymes purified from Gram-negative bacteria. PAA hydrolase-1 selectively cleaves amide bonds between ß-Asp units via an endo-type process, whereas PAA hydrolase-2 catalyzes the exo-type hydrolysis of the products of tPAA hydrolysis by PAA hydrolase-1. The novel reactivity of PAA hydrolase-1 makes it a good candidate for a biocatalyst in ß-peptide synthesis. This mini-review gives an overview of PAA hydrolases with emphasis on their biochemical and functional properties, in particular, PAA hydrolase-1. Functionally related enzymes, such as poly(R-3-hydroxybutyrate) depolymerases and ß-aminopeptidases, are compared to PAA hydrolases. This mini-review also provides findings that offer an insight into the catalytic mechanisms of PAA hydrolase-1 from Pedobacter sp. KP-2.

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We in this study investigated a novel electrochemical approach combining electro-enzyme and electrocoagulation to precipitate bisphenol A (BPA) from water containing humic acid (HA). Horseradish peroxidase was immobilized on the graphite felt of Ti electrode as HRP-GF/Ti cathode, with aluminum plate anode establishing a pair of working electrodes. BPA was 100% removed and the reduction of total organic carbon (TOC) reached 95.1% after 20-min sequencing treatment with the current density of 2.3 mA/cm(2). Real wastewater (TOC=28.76 mg/L, BPA=4.1 µg/L) also can achieve 94% BPA removal and 52% TOC reduction after sequencing treatment. Additionally, coupled electro-system with continuous flow only required energy of 0.016 kWh/m(3) to achieve simultaneous 90% BPA and 85% TOC removal. As indicated in the time-of-flight mass spectrometry and FTIR spectra, the electro-enzymatic process not only oxidized BPA into dimer and BPA-3,4-quinone, but also greatly altered the chemical and structural features of HA, where hydrophilic moieties (phenolic and alcohols) transformed into hydrophobic forms (ethers, quinone and aliphatic). These polymerized products were effectively separated from aquous solution during anodic electrocoagulation, leading to significant removal of BPA and TOC. Thus, the coupled process may provide a faster and less energy strategy to control certain emerging contaminants in water/wastewater treatment.

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Novel poly(ester-urethane)s were prepared by a synthetic route using a lipase that avoids the use of hazardous diisocyanate. The urethane linkage was formed by the reaction of phenyl carbonate with amino acids and amino alcohols that produced urethane-containing diacids and hydroxy acids, respectively. The urethane diacid underwent polymerization with polyethylene glycol and α,ω-alkanediols and also the urethane-containing hydroxy acid monomer was polymerized by the lipase to produce high-molecular-weight poly(ester-urethane)s. The periodic introduction of ester linkages into the polyurethane chain by the lipase-catalyzed polymerization afforded chemically recyclable points. They were readily depolymerized in the presence of lipase into cyclic oligomers, which were readily repolymerized in the presence of the same enzyme. Due to the symmetrical structure of the polymers, poly(ester-urethane)s synthesized in this study showed higher T(m), Young's modulus and tensile strength values.

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