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Abstract
Myrosinase (thioglucosidase, EC 3.2.1.147) is the enzyme responsible for the hydrolysis of glucosinolates (GLs). In plant tissue, myrosinase and GLs are sequestered in separate cellular compartments. As a result of cell disruption, e.g., after pathogen attack or on chopping or grinding during food preparation, the myrosinase comes into contact with GLs and catalyzes the hydrolysis of thioglucosidic bond in GL structure. Consequently, glucose is cleaved off and an unstable aglucon—thiohydroximate-O-sulfate—becomes released. Depending on the parent GLs, the hydrolysis conditions such as pH, temperature, presence of Fe2+ ions, and additional protein factors, the aglucon is converted into different classes of degradation products embracing: isothiocyanates, thiocyanates, nitriles, epithionitriles, hydroxynitriles, oxazolidine-2-thiones, or indoles. This chapter presents information on the myrosinase structure, its enzymatic activity, and the role of additional protein factors involved in the GL metabolism. In addition, we discussed methods to determine the activity of myrosinase in plant material.
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- Category:
- Monographic publication
- Type:
- rozdział, artykuł w książce - dziele zbiorowym /podręczniku w języku o zasięgu międzynarodowym
- Language:
- English
- Publication year:
- 2019
- Bibliographic description:
- Parchem K., Piekarska A., Bartoszek-Pączkowska A.: Enzymatic activities behind degradation of glucosinolates// Glucosinolates: Properties, Recovery, and Applications/ : , 2019, s.79-106
- Verified by:
- Gdańsk University of Technology
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