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- Title
Insights into glycosidic bond specificity of an engineered selective α-L-rhamnosidase N12-Rha via activity assays and molecular modelling.
- Authors
Yu, Bo; Luo, Shiyu; Ding, Yuhan; Gong, Zijie; Nie, Ting
- Abstract
αL-rhamnosidase (EC 3.2.1.40) has been widely used in food processing and pharmaceutical preparation. The recombinant α-L-rhamnosidase N12-Rha from Aspergillus niger JMU-TS528 had significantly higher catalytic activity on α-1,6 glycosidic bond than α-1,2 glycosidic bond, and had no activity on α-1,3 glycosidic bond. The activities of hydrolyzed hesperidin and naringin were 7240 U/mL and 945 U/mL, respectively, which are 10.63 times that of native α-L-rhamnosidase. The activity could maintain more than 80% at pH 3–6 and 40–60℃. Quantum chemistry calculations showed that charge difference of the C-O atoms of the α-1,2, α-1,3 and α-1,6 bonds indicated that α-1,6 bond is most easily broken and α-1,3 bond is the most stable. Molecular dynamics simulations revealed that the key residue Trp359 that may affect substrate specificity and the main catalytic sites of N12-Rha are located in the (α/α)6-barrel domain.
- Subjects
MOLECULAR dynamics; QUANTUM chemistry; ASPERGILLUS niger; CATALYTIC activity
- Publication
AMB Express, 2022, Vol 12, Issue 1, p1
- ISSN
2191-0855
- Publication type
Article
- DOI
10.1186/s13568-022-01489-5