Biochemical Characterization of Thermostable Acrylamide Amidohydrolase from Aspergillus fumigatus with Potential Activity for Acrylamide Degradation in Various Food Products.
Journal
Current microbiology
ISSN: 1432-0991
Titre abrégé: Curr Microbiol
Pays: United States
ID NLM: 7808448
Informations de publication
Date de publication:
05 Dec 2023
05 Dec 2023
Historique:
received:
15
05
2023
accepted:
30
10
2023
medline:
7
12
2023
pubmed:
6
12
2023
entrez:
5
12
2023
Statut:
epublish
Résumé
Acrylamide is the major by-product of the Maillard reactions in foods with the overheating processes of L-asparagine-rich foods with reducing sugars that usually allied with neurotoxicity and carcinogenicity. Several approaches have been used to prevent the formation of acrylamide, however, degrading the already formed acrylamide in foods remains unequivocal. Acrylamide hydrolyzing enzyme "amidohydrolase" is one of the most promising enzymes for acrylamide degradation in foods. So, amidohydrolase "amidase" from thermotolerant Aspergillus fumigatus EFBL was purified to their electrophoretic homogeneity by gel-filtration and ion-exchange chromatography, with overall purification folds 2.8 and yield 9.43%. The apparent molecular subunit structure of the purified A. fumigatus amidase was 50 kDa, with highest activity at reaction temperature of 40 °C and pH of 7.5 The enzyme displayed a significant thermal stability as revealed from the value of T
Identifiants
pubmed: 38052960
doi: 10.1007/s00284-023-03544-1
pii: 10.1007/s00284-023-03544-1
pmc: PMC10698087
doi:
Substances chimiques
Acrylamide
20R035KLCI
Amidohydrolases
EC 3.5.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
30Subventions
Organisme : Academy of Scientific Research and Technology
ID : ASRT-2023
Informations de copyright
© 2023. The Author(s).
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