Amylase is of the dextrinogenic or α-amylase type, which converts starch to dextrins. Starch is heterogenous in nature, consisting of two high molecular weight polysaccharides -Amylose and Amylopectin.

Structure of Amylose

Amylose is composed of long straight chains of glucose units joined by an α-1,4 linkage.

Structure of Amylopection

Amylopection is a branched bush like molecule of glucose units having α-1,6 glucoside linkage at the branching points.

amylase (α -amylase type) effects the random cleavage of α-1,4 linkages in amylose as well as amylopectin, forming α-maltose and leaving behind α-limit dextrins of low molecular weight, not attacked at branching points.

MODE OF ACTION of α-Amylase

Characteristics of Amylase

a) Effect of pH: Stable in the pH range of 5.0 to 7.0, being 75-100% active

b) Effect of temperature: Shows maximum activity at 55° to 60° C

For longer durations of enzyme action, temperature exceeding 37°C does not appear to be optimal. The stability study of DigeZyme® toward temperature shows that when heated for one hour at pH 7, it is stable only below 40° C, residual activity after one hour at 50° C is only about 20%.


Depending upon the pH range for optimal activity, microbial proteases are classified as:

Alkaline Proteases Active over pH 7.0 - 11.0
Neutral Proteases Active over pH 6.0 - 9.0
Acid Proteases Active over pH 2.5 - 4.0

DigeZyme® is formulated with a neutral protease with optimal stability in the pH range 6.0 - 8.0. This enzyme has a broad range of action on food proteins. Its action is similar to that of the intestinal proteolytic enzymes, which are active in the neutral to alkaline pH range.

They help to break down polypeptides into peptides and amino acids. Neutral proteases which show specificity for hydrophobic or bulky amino acid residues efficiently break down a variety of structurally different food proteins.

Characteristics of Proteases

Using the milk protein, casein, as a substrate, the characteristics of the protease contained in DigeZyme® were determined. The results revealed the presence of a neutral protease active at pH 6.0 - 8.0.

c) LACTASE Catalyses hydrolysis of terminal non reducing β-D-galactose in Lactose

d) LIPASE With olive oil as the substrate, the lipase in DigeZyme® is found to be most active at pH 7.0.

e) CELLULASE Enzyme activity is determined by measuring the formation of reducing sugar from the sodium salt of carboxymethylcellulose

Cellulase in DigeZyme® shows an optimum pH at 4.0-4.5. When incubated at 37°C for 2 hours under various conditions of pH, it shows more than 90% residual activity in the pH range 3.0-6.0.



Neutral protease