Expression of Recombinant Human α-Glucosidase in HEK293 Cells
In mammals, intestinal α-glucosidase exists as a maltase-glucoamylase complex (MGAM) and a sucrase-isomaltase complex (SI). In this study, we transiently expressed human MGAM and SI in human embryonic kidney 293 (HEK293) cells. At pH 6.0 and 37 °C, the MGAM-expressing HEK293 cells extract (MGE) exhibited maltase, glucoamylase, and isomaltase activities but not sucrase activity, whereas the SI-expressing HEK293 cells extract (SIE) exhibited sucrase, isomaltase, and maltase activities but not glucoamylase activity. The apparent <i>K</i><sub>m</sub> value of the MGE for maltose hydrolysis was 14-26% of that of the SIE for maltose, sucrose, and isomaltose hydrolysis. The respective apparent <i>V</i><sub>max</sub> values of the MGE and SIE for sucrose and isomaltose hydrolysis were 0% and 6% and 10% and 42% of those for maltose hydrolysis. These results indicated that the maltase activities of MGAM and SI were higher than those of sucrase and isomaltase.
Authors
- Emi Arikawa
- Kiyoshi Yasukawa (ORCID: https://orcid.org/0000-0001-7748-6043)
- Yuki Ikeda (ORCID: https://orcid.org/0000-0002-7371-8326)
- Masaaki Ito (ORCID: https://orcid.org/0000-0002-1101-2707)
- Teisuke Takita
- Ying Qiao (ORCID: https://orcid.org/0000-0001-9275-0113)
- Haruna Yano
- Toshiyuki Kimura (ORCID: https://orcid.org/0000-0002-1201-9943)
- So Nishimoto
- Yuki Odagaki
- Anaïs Debarbat
Institutions
- National Agriculture and Food Research Organization (JP)
- Kyoto University (JP)
- National Institute of Technology Okinawa College (JP)
Publication Details
- Journal
- Journal of Agricultural and Food Chemistry
- Published
- 2024-12-23
- DOI
- https://doi.org/10.1021/acs.jafc.4c06902
- Citations
- 2
- Primary Topic
- Digestive system and related health
- Type
- article
- Field-Weighted Citation Impact
- 1.10