Use of nuclear magnetic resonance and gas-liquid chromatography for the study of microbial nitrile-hydratases and amidases

Bui, K.; Fradet, Hugues; Thiéry, Alain; Maestracci, M.; Arnaud, A.; Galzy, P.

doi:10.1016/s0003-2670(00)81525-1

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1986

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Cited by 9 publications

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“…Enzyme assays. Amide hydrolase was assayed using a GLC apparatus to monitor the disappearance of the substrate (amide) as described by Jallageas et al (1978 b) and Bui et al (19846). Acyltransferase was assayed using the method developed by Brammar & Clarke (1964), based on the colorimetric determination of the resulting hydroxamic acids which yield red-brown complexes with Fe(II1).…”

Section: Methodsmentioning

confidence: 99%

Acyltransferase Activity of the Wide Spectrum Amidase of Brevibacterium sp. R312

Thiéry¹,

Maestracci²,

Arnaud³

et al. 1986

Microbiology

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The wide spectrum amidase from Brevibacterium sp. R3 12, which can hydrolyse many amides to the corresponding acids, was shown to transfer the acyl groups of amides, acids and esters to hydroxylamine. The transfer rates of these reactions in cytoplasmic fractions were measured and compared. The K , and V,,, were determined for different substrates in the presence of hydroxylamine. The enzyme was also shown to transfer the acyl group of the amide analogue Nmethylacetamide to hydroxylamide and that of acetamide to the hydroxylamine analogue methyl hydrox ylamine.

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Section: Methodsmentioning

confidence: 99%