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Two-step hydrolysis of amygdalin in molds
Rivista Di Biologia
|January 1, 1996
Abstract:
Mucor circinelloides LU M40 and Penicillium aurantiogriseum P 35, characterized by extracellular beta-glucosidase activity on cyanogenic glycosides, hydrolyse amygdalin by a two-step reaction mechanism being the first step of hydrolysis, from amygdalin to prunasin, very rapid (15 min) and the second one, from prunasin to mandelonitrile, much slower (120 min).
Insights
Two fungi, Mucor circinelloides and Penicillium aurantiogriseum, exhibit extracellular beta-glucosidase activity. They hydrolyze amygdalin in a two-step process, with the first step being rapid and the second much slower.
Area of Science:
- Biochemistry
- Enzymology
- Mycology
Background:
- Cyanogenic glycosides, like amygdalin, are plant-derived compounds.
- Extracellular beta-glucosidases play a role in their hydrolysis.
- Fungal enzymes are increasingly studied for biotechnological applications.
Purpose of the Study:
- To investigate the hydrolysis mechanism of amygdalin by specific fungal strains.
- To characterize the kinetics of the two-step enzymatic reaction.
Main Methods:
- Enzymatic assays using Mucor circinelloides LU M40 and Penicillium aurantiogriseum P 35.
- Analysis of hydrolysis intermediates (prunasin and mandelonitrile).
- Kinetic measurements of reaction steps.
Main Results:
- Both fungal strains possess extracellular beta-glucosidase activity.
- Amygdalin hydrolysis occurs via a two-step mechanism: amygdalin to prunasin (15 min) and prunasin to mandelonitrile (120 min).
- The second step of hydrolysis is significantly slower than the first.
Conclusions:
- Mucor circinelloides and Penicillium aurantiogriseum enzymes efficiently hydrolyze amygdalin.
- The distinct kinetics of the two hydrolysis steps provide insights into enzyme mechanisms.
- These fungi represent potential sources of beta-glucosidases for cyanogenic glycoside biotransformation.