Acid Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds under acidic pH.
AlkalineProtease is an enzyme used to break down proteins by hydrolyzing peptide bonds under alkaline pH.
Beta amylase is a form of amylase working from the non-reducing end, catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time.
Endo cellulase randomly cleaves internal bonds at amorphous sites of cellulose that create new chain ends.
Exocellulase cleaves two to four units from the ends of the exposed chains of cellulose produced by endocellulase, resulting in the tetrasaccharides or disaccharides, such as cellobiose.
Dextranases catalyze the endohydrolysis of 1,6-[[alpha]]-glucosidic linkages in dextran.
Glucoamylase is an enzyme preparation which decomposes starch into glucose by tearing-off glucose units from the non-reduced end of the polysaccharide chain.
An undefined mixture of glycolytic enzymes usually containing xylanase, mananase and other activities.
Inulinase catalyzes endohydrolysis of β−(2-1)-D-fructosidic linkages in inulin.
Invertase hydrolyzes sucrose into glucose and fructose1,2 yielding a colorless product, unlike acid hydrolysis which produces colored products
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
Pectinase is a undefined mixture of enzymes such as pectolyase, pectozyme and polygalacturonase, commonly referred to as pectic enzymes. These enzymes break down pectin, a polysaccharide substrate that is found in the cell walls of plants.
Phytase is enzyme that catalyzes the hydrolysis of phytic acid (myo-inositol hexakisphosphate), an indigestible, organic form of phosphorus that is found in grains and oil seeds and releases a usable form of inorganic phosphorus.
Pullulanase is debranching enzyme obtained from a selected fungal strain, and belongs to the group of debranching enzymes known as pullulanase.
Xylanase is an enzyme which hydrolyses xylan and releases reducing sugars as xylose equlilants.