Course title: BIOCHEMISTRY

CODE: BT156IU
Instructor: PhD. LE HONG PHU
TA: Miss Phuong Quynh
Name student: Nguyen Thi Kim Ngan
Student ID: BTBTWE18082

QUIZ 1

Score:

 Question: What do you understand about α,β, γ Amylase?

1. α-Amylases (E.C. 3.2. 1.1) are enzymes that catalyze the hydrolysis of the internal α-1,4-
glycosidic linkages in starch, converting starch into low-molecular-weight products such
as glucose, maltose, and maltotriose units.
α -amylase is widespread among living organisms. In the digestive systems of humans
and many other mammals, an alpha-amylase called ptyalin is produced by the salivary
glands, whereas pancreatic amylase is secreted by the pancreas into the small intestine.
2. β-amylase is found in bacteria, fungi, and plants; bacteria and cereal sources are the most
heat stable. β-amylase is arguably the most important enzyme as it cleaves two bound
glucose molecules (maltose) from the reducing end of the chain. The activity of β-amylase
is most important during the first stage of brewing (mashing) to produce sufficient maltose,
the most important fermentable sugar.
3. γ-Amylase: A form of amylase that cleaves the last alpha-1,4-glycosidic linkages at the
nonreducing end of amylase and amylopectin to yield glucose. It also cleaves the alpha-
1-6-glycosidic linkages. Compared to alpha- and beta-amylases, the γ-amylase is most
efficient in acidic environments.

α-Amylases β-amylase γ-Amylase

Source Animals, plants, microbes Plants, microbes Animals, microbes

Tissue Saliva, pancreas Seeds, fruits Small intestine

 Cleavage Random α-1,4 glycosidic Last α-1,4
Second α-1,4 glycosidic bond
site bond glycosidic bond

Reaction
Maltose, dextrin, etc Maltose Glucose
products

Optimum
5.6–5.8 5.4–5.5 4.0-4.5
pH

Optimum
63–68 °C (145-
temperature 68–74 °C (154-165 °F) 58–65 °C (136-149 °F)
155 °F)
in brewing