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A new colorimetric method for determining the isomerization activity of sucrose isomerase
- Authors
- Park, S.-E.; Cho, M.-H.; Lim, J.K.; Kim, J.-S.; Kim, J.H.; Kwon, D.Y.; Park, C.-S.
- Issue Date
- Dec-2006
- Publisher
- Japan Society for Bioscience Biotechnology and Agrochemistry/Nippon Nogeikagaku Kai
- Keywords
- Glucose oxidase-peroxidase; Invertase; Isomaltulose; Sucrose; Sucrose isomerase
- Citation
- Bioscience, Biotechnology and Biochemistry, v.71, no.2, pp 583 - 586
- Pages
- 4
- Indexed
- SCIE
SCOPUS
- Journal Title
- Bioscience, Biotechnology and Biochemistry
- Volume
- 71
- Number
- 2
- Start Page
- 583
- End Page
- 586
- ISSN
- 0916-8451
1347-6947
- Abstract
- A new colorimetric method for determining the isomerization activity of sucrose isomerase was developed. This colorimetric method is based on the enzymatic reactions of invertase and glucose oxidase-peroxidase (GOD-POD). The main scheme for assaying sucrose isomerase activity is to degrade sucrose in the reaction mixture to glucose and fructose by invertase and to detect the concentration of glucose generated using GOD-POD. The concentrations of trehalulose and isomaltulose, reaction products of sucrose isomerase, are calculated from the concentration of glucose. This method allows rapid and accurate determination of the isomerization activity of sucrose isomerase without inhibition by hydrolysis activity.
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