The first enzyme discovered was the Diastase.
The first enzyme discovered was the Diastase. French chemist Jean-François Persoz and Anselme Payen discovered the enzyme Diastase in 1833. Persoz and Payen extracted the enzyme from the malt solution. The name Diastase is derived from the Greek word “diastasis” (separating).
Diastase is a hydrolyzing enzyme that uses water to break the glycosidic bond between two sugar molecules. The enzyme Diastase is also known as the enzyme amylase. Three different types of amylases are α-, β-, or γ-amylase.
The Enzyme Commission number for α-Amylase is EC 220.127.116.11. The enzyme digests the α (1-4)-glycosidic bond between two glucose molecules of glycogen and starch. α-Amylase breaks carbohydrates into dextrins, maltotriose, and maltose. Humans and other mammals produce the enzyme α-Amylase. It is found in the saliva (salivary amylase) and the pancreas (Pancreatic α-amylase). The optimum pH required for enzyme activity is 6.7–7.0.
The Enzyme Commission number for α-Amylase is EC 18.104.22.168. The enzyme digests the second α-1,4 glycosidic bond which resulting into break two glucose units each time. The glucose dimer is called maltose. Bacteria, fungi, and plants produce the enzyme β-amylase. The optimum pH required for enzyme activity is 4.0–5.0. During fruit ripening, the enzyme β-amylase digests the starch into maltose.
The Enzyme Commission number for α-Amylase is EC 22.214.171.124. The enzyme digests of the α-1,6 glycosidic bond of amylose and amylopectin. Digestion of amylose and amylopectin yields glucose. Animals and microbes produce the enzyme γ-amylase. The optimum pH required for enzyme activity is around 3.0.