Oxidative degradation of UV-irradiated polyethylene by laccase-mediator system.

Polyethylene (PE) is one of the most widely used plastics. However, the chemical inertness, inefficient recycling, and random landfilling of PE waste have caused serious pollution to the natural environment. In this study, a series of laccase-mediator systems (LMS) were constructed by combination of two laccases from Botrytis aclada (BaLac) and Bacillus subtilis (BsLac) with three synthetic mediators (ABTS, HBT, and TEMPO) to oxidize LDPE films (UVPE) pretreated with high-temperature UV irradiation.

A novel salt-tolerant GH42 β-galactosidase with transglycosylation activity from deep-sea metagenome.

β-Galactosidase is a widely adopted enzyme in the food and pharmaceutical industries. Metagenome techniques have the advantage of discovering novel functional genes, particularly potential genes from uncultivated microbes. In this study, a novel GH42 β-galactosidase isolated from a deep-sea metagenome was overexpressed in Escherichia coli BL21 (DE3) and purified by affinity chromatography.

Oxidative degradation of pre-oxidated polystyrene plastics by dye decolorizing peroxidases from Thermomonospora curvata and Nostocaceae.

Biodegradation of PS has attracted lots of public attentions due to its environmental friendliness. However, no specific PS degrading enzyme has been identified yet. Dye decolorizing peroxidases (DyPs) are heme-containing peroxidases named for the ability to degrade a variety of organic dyes.

Degradation of UV-pretreated polyolefins by latex clearing protein from Streptomyces sp. Strain K30.

Plastic products made of polyethylene (PE), polypropylene (PP), and polystyrene (PS) are widely used in daily life and industrial production. Polyolefins-which have a very stable structure and do not contain any active molecular groups-are difficult to degrade and pose a serious global environment threat. This study selected latex clearing protein (Lcp) derived from Streptomyces sp.

Cloning, Expression and Characterization of a Novel Cold-adapted β-galactosidase from the Deep-sea Bacterium sp. ML52.

The bacterium sp. ML52, isolated from deep-sea water, was found to synthesize an intracellular cold-adapted β-galactosidase. A novel β-galactosidase gene from strain ML52, encoding 1058 amino acids residues, was cloned and expressed in .

Overexpression and characterization of a novel cold-adapted and salt-tolerant GH1 β-glucosidase from the marine bacterium Alteromonas sp. L82.

A novel gene (bgl) encoding a cold-adapted β-glucosidase was cloned from the marine bacterium Alteromonas sp. L82. Based on sequence analysis and its putative catalytic conserved region, Bgl belonged to the glycoside hydrolase family 1.