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Quantitative determination of α-amylase in glucoamylase preparations

✍ Scribed by J.John Marshall

Book ID
102985241
Publisher
Elsevier Science
Year
1978
Tongue
English
Weight
514 KB
Volume
85
Category
Article
ISSN
0003-2697

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✦ Synopsis

The use of modified starch substrates for the measurement of a-amylase activity is described. In the presence of excess glucoamylase, the amount of glucose released from substrates containing blockages to exo-enzyme action is proportional to the amount of cY-amylase present. The levels of a-amylase in a number of commercial glucoamylase preparations have been determined by this method. The importance of cr-amylase in achieving efficient conversion of starch into glucose is illustrated by a comparison of the time courses of degradation of amylopectin by glucoamylase preparations containing low and high levels of a-amylase.

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Synergistic action of α-amylase and gluc
Synergistic action of α-amylase and glucoamylase on hydrolysis of starch
✍ Michihiro Fujii; Yosinori Kawamura 📂 Article 📅 1985 🏛 John Wiley and Sons 🌐 English ⚖ 409 KB 👁 1 views

Synergistic action of a-amylase and glucoamylase on hydrolysis of starch is modeled by the kinetic equations presented in this paper. At the early stage of the reaction a-amylase acts as a contributor of newly formed nonreducing ends of starch molecules to glucoamylase by splitting the original star