Effects of textile dyes on health and the environment and bioremediation potential of living organisms

Chem. Pharm. Bull.(オピニオン)

Although many methods for enzyme immobilization have been described in patents and publications, relatively few processes employing immobilized enzymes have been successfully commercialized. The cost of most industrial enzymes is often only a minor component in overall process economics, and in these instances, the additional costs associated with enzyme immobilization are often not justified. More commonly the benefit realized from enzyme immobilization relates to the process advantages that an immobilized catalyst offers, for example, enabling continuous production, improved stability and the absence of the biocatalyst in the product stream. The development and attributes of several established and emerging industrial applications for immobilized enzymes, including high-fructose corn syrup production, pectin hydrolysis, debittering of fruit juices, interesterification of food fats and oils, biodiesel production, and carbon dioxide capture are reviewed herein, highlighting factors that define the advantages of enzyme immobilization.

Industrial use of immobilized enzymes

Biocatalytic potential of microorganisms have been employed for centuries to produce bread, wine, vinegar and other common products without understanding the biochemical basis of their ingredients. Microbial enzymes have gained interest for their widespread uses in industries and medicine owing to their stability, catalytic activity, and ease of production and optimization than plant and animal enzymes. The use of enzymes in various industries (e.g., food, agriculture, chemicals, and pharmaceuticals) is increasing rapidly due to reduced processing time, low energy input, cost effectiveness, nontoxic and eco-friendly characteristics. Microbial enzymes are capable of degrading toxic chemical compounds of industrial and domestic wastes (phenolic compounds, nitriles, amines etc.) either via degradation or conversion. Here in this review, we highlight and discuss current technical and scientific involvement of microorganisms in enzyme production and their present status in worldwide enzyme market.

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Microbial enzymes: industrial progress in 21st century

Edible films from pectin: Physical-mechanical and antimicrobial properties - A review

An a-L-rhamnosidase secreting fungal strain has been isolated and identified as Aspergillus clavato-nanicus MTCC-9611. The enzyme was purified to homogeneity from the culture filtrate of the fungus using concentration by ultrafiltration membrane and ion-exchange chromatography on CM-cellulose. The native PAGE analysis confirmed the homogeneity of the purified enzyme. The SDS-PAGE analysis of the purified enzyme revealed a single protein band corresponding to the molecular weight 82 kDa. The α-L-rhamnosidase activity of Aspergillus clavato-nanicus MTCC-9611 had optimum at pH 10.0 and 50°C. The Km values of the enzyme were 0.65 mM and 0.95 mM using p-nitrophenyl α-L-rhamnopyranoside and naringin as a substrates respectively. The enzyme transforms naringin to prunin at pH 10.0 and further hydrolysis of prunin to naringenin does not occur under these reaction conditions that makes α-L-rhamnosidase activity of Aspergillus clavato-nanicus MTCC-9611 promising enzyme to get prunin for pharmaceutical purposes.

α-L-rhamnosidase from Aspergillus clavato-nanicus MTCC-9611 active at alkaline pH

Summary

An α-l-rhamnosidase secreted by Penicillium citrinum MTCC-8897 has been purified to homogeneity from the culture filtrate of the fungal strain using ammonium sulphate precipitation and cation-exchange chromatography on carboxymethyl cellulose. The sodium dodecyl sulphate/polyacrylamide gel electrophoresis analysis of the purified enzyme gave a single protein band corresponding to the molecular mass 51.0 kDa. The native polyacrylamide gel electrophoresis also gave a single protein band confirming the enzyme purity. The Km and Vmax values of the enzyme for p-nitrophenyl α-l-rhamnopyranoside were 0.36 mm and 22.54 μmole min−1 mg−1, respectively, and kcat value was 17.1 s−1 giving kcat/Km value of 4.75 × 104 m−1 s−1. The pH and temperature optima of the enzyme were 7.0 and 60 °C, respectively. The purified enzyme liberated l-rhamnose from naringin, rutin, hesperidin and wine, indicating that it has biotechnological application potential for the preparation of l-rhamnose and other pharmaceutically important compounds from natural glycosides containing terminal α-l-rhamnose and also in the enhancement of wine aroma.

Purification, characterisation and application of α‐l‐rhamnosidase from Penicillium citrinum MTCC‐8897

Purification and characterization of α-l-rhamnosidase from Penicillium corylopholum MTCC-2011

Stereoselective hydroxylation of ethylbenzene to (R)-1-phenylethanol using mycelia of Aspergillus niger as catalyst

Extracellular secretion of lignin peroxidase from Pycnoporus sanguineus MTCC-137 in the liquid culture growth medium amended with lignin containing natural sources has been shown. The maximum secretion of lignin peroxidase has been found in the presence of saw dust. The enzyme has been purified to homogeneity from the culture filtrate of the fungus using ultrafiltration and anion exchange chromatography on DEAE-cellulose. The purified lignin peroxidase gave a single protein band in sodium dodecylsulphate polyacrylamide gel electrophoresis corresponding to the molecular mass 40 kDa. The K
 m, k
 cat and k
 cat/K
 m values of the enzyme using veratryl alcohol and H2O2 as the substrate were 61 M, 2.13 s−1, 3.5 × 104 M−1s−1 and 71 M, 2.13 s−1, 3.0 × 104 M−1 s−1 respectively at the optimum pH of 2.5. The temperature optimum of the enzyme was 25°C.

K. D. S. Yadav

Papers

α-L-rhamnosidase from Aspergillus clavato-nanicus MTCC-9611 active at alkaline pH

Purification, characterisation and application of α‐l‐rhamnosidase from Penicillium citrinum MTCC‐8897

Purification and characterization of α-l-rhamnosidase from Penicillium corylopholum MTCC-2011

Stereoselective hydroxylation of ethylbenzene to (R)-1-phenylethanol using mycelia of Aspergillus niger as catalyst

Purification and characterisation of lignin peroxidase from Pycnoporus sanguineus MTCC-137