Role of Musa paradisiaca ascorbate peroxidase in the transformation of methyl phenyl sulfide to its sulfoxide.
Int J Biol Macromol
; 122: 962-968, 2019 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-30408454
ABSTRACT
An ascorbate peroxidase from a new source Musa paradisiaca leaf juice has been purified to homogeneity using a simple procedure involving concentration by ultra filtration and anion exchange chromatography on diethyl amino ethyl [DEAE] cellulose column. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis [SDS-PAGE] analysis of the purified enzyme has shown a single protein band of molecular mass 208.9â¯kDa which has been confirmed by native-PAGE and intact mass analysis by mass spectrometry. The Km and kcat values of the enzyme using ascorbate and H2O2 as the variable substrates were 0.13â¯mâ¯molâ¯L-1, 40.42â¯s-1 and 0.23â¯mâ¯molâ¯L-1, 27.24â¯s-1, respectively. The pH and temperature optima of the enzyme were 7.0 and 298â¯K, respectively. The enzyme transformed approximately 97% methyl phenyl sulfide to its sulfoxide. The product was racemic mixture.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Safrol
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Sulfetos
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Musa
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Ascorbato Peroxidases
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article