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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.
α-Amylase:
The Enzyme Commission number for α-Amylase is EC 3.2.1.1. 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.
β-amylase:
The Enzyme Commission number for α-Amylase is EC 3.2.1.2. 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.
γ-Amylase:
The Enzyme Commission number for α-Amylase is EC 3.2.1.3. 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.
