Modification of the transglucosylation properties of α-glucosidases from Aspergillus oryzae and Aspergillus sojae via a single critical amino acid replacement.
Aspergillus
site-directed mutagenesis
transglucosylation
α-glucosidase
Journal
Bioscience, biotechnology, and biochemistry
ISSN: 1347-6947
Titre abrégé: Biosci Biotechnol Biochem
Pays: England
ID NLM: 9205717
Informations de publication
Date de publication:
24 Jun 2021
24 Jun 2021
Historique:
received:
01
02
2021
accepted:
11
05
2021
pubmed:
21
5
2021
medline:
10
11
2021
entrez:
20
5
2021
Statut:
ppublish
Résumé
We constructed enzyme variants of the α-glucosidases from Aspergillus oryzae (AoryAgdS) and Aspergillus sojae (AsojAgdL) by mutating the amino acid residue at position 450. AoryAgdS_H450R acquired the ability to produce considerable amounts of α-1,6-transglucosylation products, whereas AsojAgdL_R450H changed to produce more α-1,3- and α-1,4-transglucosylation products than α-1,6-products. The 450th amino acid residue is critical for the transglucosylation of these α-glucosidases.
Identifiants
pubmed: 34014266
pii: 6279032
doi: 10.1093/bbb/zbab091
doi:
Substances chimiques
alpha-Glucosidases
EC 3.2.1.20
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1706-1710Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.