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.

Molecular characterization, catalytic, kinetic and thermodynamic properties of protease produced by a mutant of Bacillus cereus-S6-3.

The proteolytic strain Bacillus cereus-S6-3 was subjected to mutagenic treatments viz. UV irradiations and methyl methane sulfonate (MMS). The obtained mutant strain, B.

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%.

Structural characterization, catalytic, kinetic and thermodynamic properties of Keratinase from Bacillus pumilus FH9.

Bacillus pumilus FH9 keratinase was purified to homogeneity with a 59.9% yield through a series of three steps. The purified enzyme was a monomeric protein with a molecular mass around 50kDa and containing 7.

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.

Structural characterization, catalytic, kinetic and thermodynamic properties of Aspergillus oryzae tannase.

Tannase (EC.3.1.

Catalytic, kinetic and thermodynamic properties of Bacillus pumilus FH9 keratinase conjugated with activated pectin.

Bacillus pumilus FH9 keratinase was covalently coupled to several oxidized polysaccharides. The conjugates were evaluated for the retained activity, kinetic and thermodynamic stability. Among all preparations, the conjugated enzyme with oxidized pectin had the highest recovered activity (71.

Catalytic and thermodynamic properties of glycosylated Bacillus cereus cyclodextrin glycosyltransferase.

Cyclodextrin glycosyltransferase (CGTase) was covalently coupled to five oxidized polysaccharides differing in structure and chemical nature. The conjugates were evaluated for the retained activity, kinetic and thermodynamic stability. The conjugated CGTase with oxidized dextran (MW 47000) had the highest retained specific activity (70.

Catalytic properties of the immobilized Aspergillus tamarii xylanase.

Xylanase from Aspergillus tamarii was covalently immobilized on Duolite A147 pretreated with the bifunctional agent glutaraldehyde. The bound enzyme retained 54.2% of the original specific activity exhibited by the free enzyme (120 U/mg protein).