Aspergillus flavus transformation of glucosinolates to nitriles by an arylsulfatase and a β-thio-glucosidase

Galletti, Stefania; Sala, E.; Leoni, Onofrio; Cinti, S.; Cerato, C.

doi:10.1016/j.soilbio.2008.01.029

Cited by 18 publications

(19 citation statements)

References 19 publications

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“…The formation of hydrolysis products formed from sinigrin in the presence of both free and immobilized MYR was evaluated by GC-MS following the method proposed by Galletti et al (2008). The enzymatic hydrolysis of both MYR forms gave comparable amounts of allylisotiocyanate as a main product and nitrile.…”

Section: Resultsmentioning

confidence: 99%

Activity of myrosinase from Sinapis alba seeds immobilized into Ca-polygalacturonate as a simplified model of soil-root interface mucigel

et al. 2010

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Ca-polygalacturonate is a demethoxylated component of pectins which are constitutive of plant root mucigel. In order to define the role of root mucigel in myrosinase immobilization and activity at root level, a myrosinase enzyme which had been isolated from Sinapis alba seeds was immobilized into Capolygalacturonate. The activity profile for the immobilized and free enzyme was evaluated using the pH-Stat method as a function of time, temperature, and pH. The Michaelis-Menten kinetic parameters change between the immobilized (V max =127±13 U mg −1 protein; K M =6.28±0.09mM) and free (V max =17±1 U mg −1 protein; K M =0.96±0.01mM) forms of myrosinase, probably due to conformational changes involving the active site as a consequence of enzyme immobilization. Immobilized enzyme activity evaluated as a function of different substrates gave the highest value with nasturtin, the glucosinolate that is typical of several brassicaceae plant roots containing the glucosinolatemyrosinase defensive system. No feedback regulation mechanism was found in the presence of an excess of enzymatic reaction products (i.e. allyl isothiocyanate or sulphate). The high enzyme immobilization yield into Ca-polygalacturonate and its activity preservation under different conditions suggest that the enzyme released by plants at root level could be entrapped in root mucigel in order to preserve its activity.

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Section: Resultsmentioning

confidence: 99%

Activity of myrosinase from Sinapis alba seeds immobilized into Ca-polygalacturonate as a simplified model of soil-root interface mucigel

et al. 2010

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“…Several studies have already reported the presence of myrosinase in Aspergillus niger [78,79] and other fungi. [80,81]…”

Section: Diversity Of Microorganisms Able To Metabolize Glucosinolatesmentioning

confidence: 99%

“…In this review, 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 metabolize GSLs. Several studies have already reported the presence of myrosinase in Aspergillus niger and other fungi …”

Section: Introductionmentioning

confidence: 99%

Gut Glucosinolate Metabolism and Isothiocyanate Production

Narbad

Rossiter

2018

Molecular Nutrition Food Res

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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.

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“…Indeed, specialised fungi have recently been reported to metabolise glucosinolates to desulfoglucosinolates and subsequently nitriles (Galletti et al, 2008), and generalist lepidopteran insects preferentially feed on Arabidopsis thaliana plants with nitrile-specifying activity (Lambrix et al, 2001;Burow et al, 2006). As nitriles may also be formed after human consumption of crucifers due to epithiospecifier protein (Matusheski et al, 2006) or plant-encoded NSPs (Kissen and Bones, 2009;Burow et al, 2009), nitrile metabolism may also be of interest in the investigation of glucosinolate effects in human nutrition.…”

Section: Perspectivesmentioning

confidence: 99%

Complex metabolism of aromatic glucosinolates in Pieris rapae caterpillars involving nitrile formation, hydroxylation, demethylation, sulfation, and host plant dependent carboxylic acid formation

Agerbirk

Olsen

Poulsen

et al. 2010

Insect Biochemistry and Molecular Biology

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Aspergillus flavus transformation of glucosinolates to nitriles by an arylsulfatase and a β-thio-glucosidase

Cited by 18 publications

References 19 publications

Activity of myrosinase from Sinapis alba seeds immobilized into Ca-polygalacturonate as a simplified model of soil-root interface mucigel

Activity of myrosinase from Sinapis alba seeds immobilized into Ca-polygalacturonate as a simplified model of soil-root interface mucigel

Gut Glucosinolate Metabolism and Isothiocyanate Production

Complex metabolism of aromatic glucosinolates in Pieris rapae caterpillars involving nitrile formation, hydroxylation, demethylation, sulfation, and host plant dependent carboxylic acid formation

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