Modelization and implementation of free adsorption and electrosorption of Cr (VI) from wastewater using AlO nanoparticles: assessment and comparison of the two processes.

The objective of this study was to apply the technique of electrosorption in order to assess the capacity of heterogeneous adsorption under an electric field. This was to enhance the adsorption capacity of the nanoparticles, to shorten the adsorption time, and to reduce the cost of the purification of contaminated waters. A final objective of this study was to compare the free adsorption (FA) and the electrosorption (ES) to understand the interface adsorbent/adsorbate at different contact conditions.

Biochemical and molecular characterisation of a new alkaline trypsin from Liza aurata: Structural features explaining thermal stability.

This study investigated the fine structure and biochemical characterization of trypsin from the viscera of Liza aurata. The purified enzyme displayed an apparent molecular weight of 23 kDa as determined by sodium dodecyl sulphate-polyaccrylamide gel electrophoresis (SDS-PAGE). The optimum pH and temperature for the proteolytic activity were 10.

Composition, functional properties and in vitro antioxidant activity of protein hydrolysates prepared from sardinelle (Sardinella aurita) muscle.

Composition, functional properties and in vitro antioxidative activities of protein hydrolysates prepared from muscle of sardinelle (Sardinella aurita) were investigated. Sardinelle protein hydrolysates (SPH) were obtained by treatment with crude enzyme preparations from Bacillus pumilus A1 (SPHA1), Bacillus mojavensis A21 (SPHA21) and crude enzyme extract from sardinelle (Sardinella aurita) viscera (SPHEE). The protein hydrolysates SPHA1, SPHA21 and SPHEE contained high protein content 79.

Pseudomonas aeruginosa A2 elastase: purification, characterization and biotechnological applications.

An extracellular protease from Pseudomonas aeruginosa A2 grown in media containing shrimp shell powder as a unique source of nutriments was purified and characterized. The enzyme was purified to homogeneity from culture supernatant by ultrafiltration, Sephadex G-100 gel filtration and Sepharose Mono Q anion exchange chromatography, with a 2.23-fold increase in specific activity and 64.

Purification and characterization of three trypsin isoforms from viscera of sardinelle (Sardinella aurita).

Three trypsin isoforms A, B and C were purified to homogeneity from the viscera of sardinelle (Sardinella aurita). Purification was achieved by ammonium sulfate precipitation (20-70% (w/v)), Sephadex G-100 gel filtration and Mono Q-Sepharose anion-exchange chromatography. The molecular weights of these purified enzymes were estimated to be 28.

Alkaline chymotrypsin from striped seabream (Lithognathus mormyrus) viscera: purification and characterization.

An alkaline chymotrypsin from the intestine of striped seabream (Lithognathus mormyrus) was purified by precipitation with ammonium sulfate, Sephadex G-100 gel filtration, Mono Q-Sepharose anion-exchange chromatography, ultrafiltration, second Sephadex G-100 gel filtration, and a second Mono Q-Sepharose anion-exchange chromatography with a 80-fold increase in specific activity. The molecular weight of the purified alkaline chymotrypsin was estimated to be 27 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and size exclusion chromatography. The enzyme was highly active over a wide range of pH from 7.