Commercialization potential of PET (polyethylene terephthalate) recycled nanomaterials: A review on validation parameters.

Polyethylene Terephthalate (PET) is a polymer which is considered as one of the major contaminants to the environment. The PET waste materials can be recycled to produce value-added products. PET can be converted to nanoparticles, nanofibers, nanocomposites, and nano coatings.

Cloning, expression and characterization of laccase from Bacillus licheniformis NS2324 in E. coli application in dye decolorization.

Laccase gene from Bacillus licheniformis NS2324 was cloned and expressed in E. coli by using pUC 18 as cloning vector and pet 15b as expression vector. The purified recombinant laccase (rLacNS2324) showed a molecular mass of 66 KDa.

Purification and characterization of a novel white highly thermo stable laccase from a novel Bacillus sp. MSK-01 having potential to be used as anticancer agent.

Laccases are multicoopper oxidases catalyzing the oxidation of phenolic as well as non-phenolic compounds. Laccases show typical blue color due to the presence of covalent Type 1 Cu-Cys bond which absorbs at 600 nm. However, recently some white laccases have also been identified which lacks typical spectra of blue laccases and do not show peak at 600 nm.

Lignolytic and hemicellulolytic enzyme cocktail production from Bacillus tequilensis LXM 55 and its application in pulp biobleaching.

Bioprocessing of pulp requires lignolytic as well as hemicellulolytic enzymes. The present study is the first report of a cocktail of laccase (L), xylanase (X), and mannanase (M), from a single bacterium for pulp biobleaching. A novel strain Bacillus tequilensis LXM 55 produced thermo-alkali stable L + X + M.

Response surface based optimization of laccase production from MSK-01 using fruit juice waste as an effective substrate.

Laccases are multicopper oxidases containing four copper atoms per monomer distributed in three redox sites. Because of its tremendous applications in different areas, isolation of new laccases with wide range of industrial implementation. The present study focuses on the optimization of laccase production from sp.

Immobilization of laccase-ABTS system for the development of a continuous flow packed bed bioreactor for decolorization of textile effluent.

Decolourization of textile effluent is always being a problem of major concern for the safe disposal of effluent water in river stream. Due to intense colour of the effluent water, even after the treatment, disposal of the water in river stream is under strict environmental regulation. Laccase, a natural oxidase, have the miraculous power to decolourize different dyes with or without mediators.

An alkaline bacterial laccase for polymerization of natural precursors for hair dye synthesis.

In the present study, an extracellular alkali stable laccase (Lac DS) from DS which has pH optima at 8.5 using -phenylenediamine (PPD) as substrate has been reported. Lac DS retained 70% activity for 4 h at pH 8.

An extracellular thermo-alkali-stable laccase from Bacillus tequilensis SN4, with a potential to biobleach softwood pulp.

Degradation of residual lignin in kraft pulp by chemical bleaching is implicated in causing environmental pollution. The use of thermo- and alkali-tolerant bacterial laccases is considered to be important biological alternative to chemical processing. Laccases from Bacillus species have shown promise in this respect but their intracellular/spore bound presence make their industrial application economically unfeasible.

Lime and Sulphide-Free Dehairing of Animal Skin Using Collagenase-Free Alkaline Protease from Vibrio metschnikovii NG155.

The objective of this work was to isolate a microorganism producing alkaline protease that can be used as an ecofriendly alternative to chemicals in dehairing process of leather manufacture. Alkaline protease producing bacterium Vibrio metschnikovii NG155 was isolated from soil samples of leather industry. The protease was highly effective in dehairing of goat skin, completely eliminating the use of lime and sulfide.

Purification and characterization of an extracellular, thermo-alkali-stable, metal tolerant laccase from Bacillus tequilensis SN4.

A novel extracellular thermo-alkali-stable laccase from Bacillus tequilensis SN4 (SN4LAC) was purified to homogeneity. The laccase was a monomeric protein of molecular weight 32 KDa. UV-visible spectrum and peptide mass fingerprinting results showed that SN4LAC is a multicopper oxidase.