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Last Updated February 18th 2020, 7:48:33 pm

Sulforaphane is an isothiocyanate, formed from hydrolysis of glucoraphanin (a major glucosinolate in broccoli).[1]

Biological Activity

Microflora in the human gut can hydrolyse glucosinolates into bioactive isothiocyanate compounds such as sulforaphane.[1:1]

Healing Properties

Disease / Symptom Treatment

  1. Study Type: Plant Study
    Title: A Comparison of Myrosinase Activity and Stability in Fresh Broccoli (B. oleracea var. Italica) and Brown Mustard (B. juncea) Seeds
    Author(s): Okunade, Olukayode Adediran, Methven, Lisa, Niranjan, Keshavan
    Institution(s): Department of Food Science & Technology, Federal Polytechnic Ado Ekiti. Nigeria; Department of Food & Nutritional Sciences, University of Reading, Whiteknights, Reading, U.K.
    Publication: Turkish Journal of Agriculture - Food Science and Technology
    Date: 09/13/2019
    Abstract: The effects of temperature and pressure processing on myrosinase extracted from fresh broccoli and brown mustard seed was studied. Brown mustard seeds had higher myrosinase activity (2.75 un/mL) than fresh broccoli (0.58 un/mL). The extent of enzyme inactivation increased with pressure (200- 800 MPa) and temperature (30-80°C) for both brown mustard seeds and fresh broccoli myrosinase. However, at combinations of lower pressures (200-400 MPa) and temperatures (30-80°C), there was less myrosinase inactivation. When processing at a pressure of 300 MPa with a temperature of 70°C for 10 minutes, there was 65% myrosinase activity for brown mustard while at 300 MPa and 60°C, activity retention in fresh broccoli was 30%. Whereas, the corresponding activity retentions when applying only heat (70°C for 10 minutes) was 35% for brown mustard myrosinase, while there was no measurable myrosinase activity for fresh broccoli (60°C, 10 minutes). Thus, application of moderate pressures (200-400 MPa) on brown mustard and fresh broccoli can potentially be used to retain myrosinase activity needed for subsequent glucosinolate hydrolysis.
    Link: Source
    Citations: ↩︎ ↩︎