Abstract

The glucosinolate‐myrosinase system in plants has been well studied over the years while relatively little research has been undertaken on the bacterial metabolism of glucosinolates. The products of myrosinase‐based glucosinolate hydrolysis in the human gut are important to health, particularly the isothiocyanates, as they are shown to have anticancer properties as well as other beneficial roles in human health. This review is concerned with the bacterial metabolism of glucosinolates but is not restricted to the human gut. Isothiocyanate production and nitrile formation are discussed together with the mechanisms of the formation of these compounds. Side chain modification of the methylsulfinylalkyl glucosinolates is reviewed and the implications for bioactivity of the resultant products are also discussed.

Highlights

  • During the cooking process of cruciferous vegetables, myrosinase activity and associated protein specifier proteins are usually destroyed unless strict cooking times are adhered to [1]

  • Further work [23] with other bacteria showed the same trend with the exception of L. agilis R16 and E. casseliflavus CP1 which could not metabolise glucoraphanin or glucoiberin while E. coli VL8 was able to biotransform both of these GSLs as well as others (Table 2)

  • We have focused only on bacterial metabolism but it is highly likely that in time we will discover other microbes, archaea, yeast and fungi that are able to metabolise GSLs

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Summary

Introduction

During the cooking process of cruciferous vegetables, myrosinase activity and associated protein specifier proteins are usually destroyed unless strict cooking times are adhered to [1]. A detailed study examining the metabolism of five DS-GSLs in bacterial fermentations has recently been reported [24] where it was shown that specific strains of E. coli VL8, L. agilis R16 and E. casseliflavus CP1 can utilize DS-GSLs as a carbon source and produce nitriles. Further work [23] with other bacteria showed the same trend with the exception of L. agilis R16 and E. casseliflavus CP1 which could not metabolise glucoraphanin or glucoiberin while E. coli VL8 was able to biotransform both of these GSLs as well as others (Table 2) It was observed in this study that both sulforaphane and sulforaphane nitrile were able to undergo this conversion to the reduced forms. Several studies have already reported the presence of myrosinase in Aspergillus niger [79, 80] and other fungi [81, 82]

Conclusions and future work
Findings
Graphic Abstract
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