Studies on myrosinases III. Enzymatic properties of myrosinases from Sinapis alba and Brassica napus seeds

Rune Björkman, Bo Lönnerdal

Research output: Contribution to journalArticle

80 Scopus citations

Abstract

A comparative study was performed on some enzymatic properties of myrosinase isoenzymes (thioglucoside glucohydrolases, EC 3.2.3.1) from white mustard seed (Sinapis alba) and rapeseed Brassica napus). The investigation comprised the determination of pH optima, temperature maxima and the enzymatic stabilities of the isoenzymes, when temperature, pH, buffer and time were varied. The effect of ascorbic acid on the kinetic constants Km and V was found to be different for the isoenzymes. Comparative studies were also made of the activities of the isoenzymes on various glucosinolates, and the myrosinase activities in a number of cultivars of B. napus, Brassica campestris and S. alba. The results indicate that there are both physicochemical and enzymatic differences between myrosinase isoenzymes and that a large amounty of variance exists. They are, however, likely to have the same genetic origin. No significant variation in substrate specificity was found among the isoenzymes.

Original languageEnglish (US)
Pages (from-to)121-131
Number of pages11
JournalBBA - Enzymology
Volume327
Issue number1
DOIs
StatePublished - Nov 15 1973
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

Fingerprint Dive into the research topics of 'Studies on myrosinases III. Enzymatic properties of myrosinases from Sinapis alba and Brassica napus seeds'. Together they form a unique fingerprint.

  • Cite this