Clay-enzyme complexes and method for preparing same

DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS In accordance with the present invention, there are provided novel immobilized enzyme compositions comprising enzyme-organoclay complexes which are substantially pH independent and wherein the catalytic activity of the immobilized enzymes may be substantially comparable to the activity of the free enzyme in a homogeneous solution.
The enzymes to which the present invention is applicable for preparing the novel immobilized enzyme compositions of the invention can be any enzyme known in the art.
Enzymes are catalysts elaborated by living organisms that control the many processes associated with life.
Many have high specificity with respect to the substances (substrates) whose reactions they catalyze; hence they are usually named by addition of the suffix "ase" to the root of the name of the substrate.
They are all proteins, although some contain a nonproteinoid prosthetic group essential for activity.
Enzymes fall into two broad divisions: hydrolases, which control hydrolysis (and resynthesis) of esters, carbohydrates, proteins, amides; and enzymes that control various oxidation-reduction reactions.
Almost all enzymes show stereochemical specificity.
A few, such as urease, have absolute specificity in that they control the reaction of only one substrate.
Certain enzymes show only linkage specificity; for example, there are esterases capable of promoting hydrolysis of any ester regardless of the structures of the acid and alcohol components.
The more usual requirements fall in between the absolute and the linkage type, that is, the enzyme requires a specific linkage and also that certain functional groups be in the vicinity of this linkage.
It has been found that various proteinases have definite requirements in order to catalyze hydrolysis of peptide bonds.
A majority of proteolytic enzymes such as pepsin and trypsin are endopeptidesis which attack centrally located peptide bonds; while some such as carboxypeptides, affect only terminal peptide bonds