当前位置： SCI文献检索 > APPLIED MICROBIOLOGY AND BIOTECHNOLOGY期刊下所有文献 > A novel Aspergillus oryzae diglycosidase that hydrolyzes 6-O-α-L-rhamnosyl-β-D-glucoside from flavonoids.

A novel Aspergillus oryzae diglycosidase that hydrolyzes 6-O-α-L-rhamnosyl-β-D-glucoside from flavonoids.

Abstract：

:α-L-Rhamnosyl-β-D-glucosidase (rutinosidase) hydrolyzes the glycosidic linkage between the disaccharide 6-O-α-L-rhamnosyl-β-D-glucoside (rutinose) and the aglycone. We identified a hypothetical protein (annotated as AO090012000917) encoded in the Aspergillus oryzae genome that exhibits sequence similarity with Aspergillus niger rutinosidase. The recombinant enzyme was expressed in Pichia pastoris GS115 and purified as a glyco-protein with apparent molecular mass of 65-75 kDa by SDS-PAGE. After N-deglycosylation, we observed a 42- and 40-kDa band, representing proteins before and after N-terminal signal peptide processing, respectively. Optimal enzymatic activity was observed at pH 4.0 and temperature of 45 °C. This enzyme is also significantly thermo-stable, with 90% activity retained after 1 h at 45 °C and 70% activity retained after 4 h, even at 50 °C. Biochemical characterization revealed that the enzyme has higher substrate specificity for 3-O-linked flavonoid β-rutinosides like rutin and kaempferol-3-O-rutinoside, than for 7-O-linked flavonoid β-rutinoside like hesperidin. However, no activity was found with naringin, diosmin, monoglycosylated chromogenic substrates, and polymeric laminarin substrate. Kinetic analyses showed that K m value toward rutin was higher than those toward hesperidin and kaempferol-3-O-rutinoside. Meanwhile, kcat value toward hesperidin was lower than those toward kaempferol-3-O-rutinoside and rutin. Overall, the catalytic efficiency (kcat/K m ) was highest for kaempferol-3-O-rutinoside.

journal_name

Appl Microbiol Biotechnol

journal_title

Applied microbiology and biotechnology

authors

Ishikawa M,Kawasaki M,Shiono Y,Koseki T

doi

10.1007/s00253-018-8840-9

subject

Has Abstract

pub_date

2018-04-01 00:00:00

pages

3193-3201

issue

7

eissn

0175-7598

issn

1432-0614

pii

10.1007/s00253-018-8840-9

journal_volume

102

pub_type

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