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- Title
Isoflavone aglycones production from isoflavone glycosides by display of β-glucosidase from Aspergillus oryzae on yeast cell surface.
- Authors
Kaya, Masahiko; Ito, Junji; Kotaka, Atsushi; Matsumura, Kengo; Bando, Hiroki; Sahara, Hiroshi; Ogino, Chiaki; Shibasaki, Seiji; Kuroda, Kouichi; Ueda, Mitsuyoshi; Kondo, Akihiko; Hata, Yoji
- Abstract
For efficient production of isoflavone aglycones from soybean isoflavones, we isolated three novel types of β-glucosidase (BGL1, BGL3, and BGL5) from the filamentous fungi Aspergillus oryzae. Three enzymes were independently displayed on the cell surface of a yeast Saccharomyces cerevisiae as a fusion protein with α-agglutinin. Three β-glucosidase-displaying yeast strains hydrolyzed isoflavone glycosides efficiently but exhibited different substrate specificities. Among these β-glucosidases, BGL1 exhibited the highest activity and also broad substrate specificity to isoflavone glycosides. Although glucose released from isoflavone glycosides are generally known to inhibit β-glucosidase, the residual ratio of isoflavone glycosides in the reaction mixture with BGL1-displaying yeast strain (Sc-BGL1) reached approximately 6.2%, and the glucose concentration in the reaction mixture was maintained at lower level. This result indicated that Sc-BGL1 assimilated the glucose before they inhibited the hydrolysis reaction, and efficient production of isoflavone aglycones was achieved by engineered yeast cells displaying β-glucosidase.
- Subjects
ISOFLAVONES; GLYCOSIDES; GLUCOSIDASES; CELL membranes; HYDROLYSIS; ASPERGILLUS; YEAST; LEAVENING agents; IPRIFLAVONE
- Publication
Applied Microbiology & Biotechnology, 2008, Vol 79, Issue 1, p51
- ISSN
0175-7598
- Publication type
Article
- DOI
10.1007/s00253-008-1393-6