The catalytic and kinetic characterization of Bacillus subtilis MK775302 milk clotting enzyme: comparison with calf rennet as a coagulant in white soft cheese manufacture.

Background: Calf rennet is considered the traditional source of milk clotting enzyme (MCE). However, increasing cheese consumption with decreasing the calf rennet supply had encouraged the quest for new rennet alternatives. The purpose of this study is to acquire more information about the catalytic and kinetic properties of partially purified Bacillus subtilis MK775302 MCE and to assess the role of enzyme in cheese manufacture.

Production of a novel laccase from Ceratorhiza hydrophila and assessing its potential in natural dye fixation and cytotoxicity against tumor cells.

Background: Flavonoid natural dyes have gained attention because they are nontoxic and eco-friendly. However, they do not work effectively with artificial fibers and require the use of mordants, which are considered as hazardous chemicals. Laccase enzyme catalyzes the oxidation of phenols, forming phenoxyl radicals that undergo a further polymerization process.

Rice straw and orange peel wastes as cheap and eco-friendly substrates: A new approach in β-galactosidase (lactase) enzyme production by the new isolate L. paracasei MK852178 to produce low-lactose yogurt for lactose-intolerant people.

Converting wastes to valuable products is the main target for many kinds of research nowadays. Wastes represent an environmental problem and getting rid of it is not easy and causes pollution. Accordingly, this study offers production of the valuable enzyme β-galactosidase using rice straw and orange peel as the main medium constituents.

Improving the catalytic, kinetic and thermodynamic properties of Bacillus subtilis KU710517 milk clotting enzyme via conjugation with polyethylene glycol.

Milk clotting enzyme (MCE) produced by Bacillus subtilis KU710517 was conjugated to several activated polysaccharides. Among all the conjugates, the enzyme conjugated with polyethylene glycol (PEG) exhibited the highest retained activity (551U/mg protein) with a recovered activity of 95.3%.

Catalytic, kinetic and thermodynamic properties of stabilized Bacillus stearothermophilus alkaline protease.

Bacillus stearothermophilus alkaline protease was conjugated to several oxidized polysaccharides of different chemical structure. The conjugates were evaluated for the kinetic and thermodynamic stability. The conjugated enzyme with oxidized pectin had the highest retained activity (79.

Optimization of inulinase production from low cost substrates using Plackett-Burman and Taguchi methods.

Four marine-derived fungal isolates were screened for the production of inulinase enzyme from low cost substrates under solid state fermentation (SSF), one of them identified as Aspergillus terreus showed the highest inulinase activity using artichoke leaves as a solid substrate. Sequential optimization strategy, based on statistical experimental designs was employed to optimize the composition of the medium, including Plackett-Burman and Taguchi's (L9 3(4)) orthogonal array designs. Under the optimized conditions, inulinase activity (21.