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Published in 2022 at "Applied Biochemistry and Biotechnology"
DOI: 10.1007/s12010-022-03894-9
Abstract: Aspergillus niger has been used for homologous and heterologous expressions of many protein products. In this study, the α-L-rhamnosidase from A. niger (Rha-N1, GenBank XP_001389086.1) was homologously expressed in A. niger 3.350 by Agrobacterium tumefaciens-mediated…
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Keywords:
aspergillus niger;
characterization rhamnosidase;
homologous expression;
transformation ... See more keywords
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Published in 2018 at "Archives of biochemistry and biophysics"
DOI: 10.1016/j.abb.2018.04.013
Abstract: α-L-Rhamnosidases (α-RHAs, EC 3.2.1.40) are glycosyl hydrolases (GHs) hydrolyzing terminal α-l-rhamnose residues from different substrates such as heteropolysaccharides, glycosylated proteins and natural flavonoids. Although the possibility to hydrolyze rhamnose from natural flavonoids has boosted the…
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Keywords:
natural flavonoids;
functional insights;
novosphingobium pp1y;
structural functional ... See more keywords
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Published in 2018 at "Bioorganic chemistry"
DOI: 10.1016/j.bioorg.2018.08.004
Abstract: In this study, a α-l-rhamnosidase gene from Bacteroides thetaiotaomicron VPI-5482 was cloned and expressed in Escherichia coli. The specific activity of rhamnosidase was 0.57 U/mg in LB medium with 0.1 mM Isopropyl β-d-Thiogalactoside (IPTG) induction at…
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Keywords:
bacteroides thetaiotaomicron;
rhamnoside rhamnoside;
epimedin;
rhamnosidase ... See more keywords
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Published in 2020 at "Chemical Physics Letters"
DOI: 10.1016/j.cplett.2020.137695
Abstract: Abstract Recently, a kind of α-L-rhamnosidase from Bacteroides thetaiotaomicron (BtRha) was characterized and studied for the hydrolysis of natural substrates. In order to investigate catalytic specificity of BtRha, three natural substrates, epimedin C, naringin, and…
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Keywords:
bacteroides thetaiotaomicron;
docking dynamics;
catalytic specificity;
rhamnosidase ... See more keywords
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Published in 2018 at "Journal of biotechnology"
DOI: 10.1016/j.jbiotec.2018.03.013
Abstract: The α-L-Rhamnosidase is an important enzyme with applications in the food and pharmaceutical industries because it can release terminal L-rhamnose residues from various natural products. In this study, the B-factor-saturation mutagenesis strategy was used to…
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Keywords:
d594q g827k;
g827k d594q;
thermostability;
d594q mutant ... See more keywords
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Published in 2019 at "Journal of agricultural and food chemistry"
DOI: 10.1021/acs.jafc.8b06932
Abstract: α-L-Rhamnosidase is a glycoside hydrolase capable of removing naringin from citrus juice. However, α-L-rhamnosidases always have broad substrate spectra, causing negative effects on citrus juice. In this study, a α-L-rhamnosidase-expressing fungal strain, JMU-TS529, was identified,…
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Keywords:
clade aspergillus;
new clade;
rhamnosidase;
citrus juice ... See more keywords
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Published in 2022 at "Journal of Fungi"
DOI: 10.3390/jof8060644
Abstract: Icariin is the most effective bioactive compound in Herba Epimedii. To enhance the content of icariin in the epimedium water extract, a novel strain, Papiliotrema laurentii ZJU-L07, producing an intracellular α-L-rhamnosidase was isolated from the…
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Keywords:
rhamnosidase;
icariin;
laurentii zju;
production icariin ... See more keywords
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Published in 2022 at "Journal of Fungi"
DOI: 10.3390/jof8111181
Abstract: In Aspergillus nidulans L-rhamnose is catabolised to pyruvate and L-lactaldehyde, and the latter ultimately to L-lactate, via the non-phosphorylated pathway (LRA) encoded by the genes lraA-D, and aldA that encodes a broad substrate range aldehyde…
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Keywords:
rhamnosidase;
loss function;
loss;
production ... See more keywords