Modification of the transglucosylation properties of α-glucosidases from Aspergillus oryzae and Aspergillus sojae via a single critical amino acid replacement

Biosci Biotechnol Biochem. 2021 Jun 24;85(7):1706-1710. doi: 10.1093/bbb/zbab091.

Abstract

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.

Keywords: Aspergillus; site-directed mutagenesis; transglucosylation; α-glucosidase.

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution*
  • Aspergillus / enzymology*
  • Aspergillus oryzae / enzymology*
  • Glycosylation
  • Sequence Homology, Amino Acid
  • alpha-Glucosidases / chemistry
  • alpha-Glucosidases / metabolism*

Substances

  • alpha-Glucosidases

Supplementary concepts

  • Aspergillus sojae