Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk.

Enzymatic milk coagulation for cheese manufacturing involves the cleavage of the scissile bond in kappa-casein by an aspartic acid protease. Bovine chymosin is the preferred enzyme, combining a strong clotting activity with a low general proteolytic activity. In the present study, we report expression and enzymatic properties of recombinant camel chymosin expressed in Aspergillus niger.

Purification and structural characterization of 3-hydroxypropionaldehyde and its derivatives.

The compound 3-hydroxypropionaldehyde (3-HPA), together with HPA hydrate and HPA dimer, in aqueous solution forms a system with interesting chemical properties. Therefore, 3-HPA has attracted attention by the chemical industry for use as a precursor in the production of plastics, acrylic acid, and 1,3-propanediol and by the food industry, in using 3-HPA-producing Lactobacillus reuteri as a probiotic. To produce 3-HPA in high yield from glycerol, L.