THE EFFECT OF L-ASCORBIC ACID ON MYROSINASE ACTIVITY

The addition of 10-2 to 10-3M L-ascorbic acid to the reaction medium was found to greatly promote the white mustard myrosinase activity under the condition (pH 6.4), producing neither white turbidity nor hydrogen sulfide. The amount of the white turbidity and hydrogen sulfide produced on addition of...

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Bibliographic Details
Published inJournal of vitaminology Vol. 10; no. 1; pp. 44 - 54
Main Authors KOJIMA, MISAO, TAMIYA, KEIKO
Format Journal Article
LanguageEnglish
Published Japan THE VITAMIN SOCIETY OF JAPAN 01.01.1964
Subjects
Amylases
Ascorbic Acid
Aspergillus
Chemical Phenomena
Chemistry
Chloromercuribenzoates
Coenzymes
Cysteine
Enzyme Inhibitors
Gallic Acid
Glutathione
Glycoside Hydrolases
Hydrogen-Ion Concentration
Mustard Plant
OldMedline
Spectrum Analysis
Sulfatases
ENZYME INHIBITORS
EXPERIMENTAL LAB STUDY
CYSTEINE
HYDROGEN-ION CONCENTRATION
COENZYMES
SPECTRUM ANALYSIS
ASCORBIC ACID
MUSTARD
ASPERGILLUS
SULFATASES
GALLIC ACID
GLUTATHIONE
AMYLASE
CHEMISTRY
CHLOROMERCURIBENZOATES
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ISSN0022-5398
DOI10.5925/jnsv1954.10.44

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Summary:The addition of 10-2 to 10-3M L-ascorbic acid to the reaction medium was found to greatly promote the white mustard myrosinase activity under the condition (pH 6.4), producing neither white turbidity nor hydrogen sulfide. The amount of the white turbidity and hydrogen sulfide produced on addition of ascorbic acid to the reaction mixture of myrosinase and sinigrin increased with the decrease of the pH value of the medium. Any of those materials was produced in a larger amount in the case of white mustard enzyme than in the case of mold enzyme. The material producing white turbidity was found to be composed mainly of protein. It may be concluded that ascobic acid is a specific activator of myrosinase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0022-5398
DOI:10.5925/jnsv1954.10.44