Results 1 to 10 of about 1,494 (149)

L-Rhamnose induction of Aspergillus nidulans α-L-rhamnosidase genes is glucose repressed via a CreA-independent mechanism acting at the level of inducer uptake [PDF]

open access: yesMicrobial Cell Factories, 2012
Background Little is known about the structure and regulation of fungal α-L-rhamnosidase genes despite increasing interest in the biotechnological potential of the enzymes that they encode.
Tamayo-Ramos Juan A   +4 more
doaj   +6 more sources

Multiple Enzymes Expressed by the Gut Microbiota Can Transform Typhaneoside and Are Associated with Improving Hyperlipidemia [PDF]

open access: yesAdvanced Science
The mechanism of multiple enzymes mediated drug metabolism in gut microbiota is still unclear. This study explores multiple enzyme interaction process of typhactyloside (TYP) with gut microbiota and its lipid‐lowering pharmacological activity.
Hui Xu   +11 more
doaj   +3 more sources

The influence of coordinative tartrate and malatogermanate compounds on the activity of α-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus [PDF]

open access: yesThe Ukrainian Biochemical Journal, 2020
Recently enzyme preparations of microbial origin become increasingly important in different industries. Preparations of α-L-rhamnosidase are used in the pharmaceutical industry as well as in scientific work as a tool for analytical research.
О. V. Gudzenko   +5 more
doaj   +3 more sources

Computational design of Lactobacillus Acidophilus α-L-rhamnosidase to increase its structural stability. [PDF]

open access: yesPLoS ONE, 2022
α-L-rhamnosidase catalyzes hydrolysis of the terminal α-L-rhamnose from various natural rhamnoglycosides, including naringin and hesperidin, and has various applications such as debittering of citrus juices in the food industry and flavonoid ...
Thassanai Sitthiyotha   +4 more
doaj   +3 more sources

Insights into glycosidic bond specificity of an engineered selective α-L-rhamnosidase N12-Rha via activity assays and molecular modelling [PDF]

open access: yesAMB Express, 2022
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 ...
Bo Yu   +4 more
doaj   +2 more sources

The Loss-of-Function Mutation aldA67 Leads to Enhanced α-L-Rhamnosidase Production by Aspergillus nidulans [PDF]

open access: yesJournal of Fungi, 2022
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 ...
Margarita Orejas, Andrew P. MacCabe
doaj   +2 more sources

Purification and Characterization of a Novel α-L-Rhamnosidase from Papiliotrema laurentii ZJU-L07 and Its Application in Production of Icariin from Epimedin C [PDF]

open access: yesJournal of Fungi, 2022
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 soil ...
Hanghang Lou   +3 more
doaj   +2 more sources

Activity of an A-L-Rhamnosidase Produced by Aspergillus niger During Solid State Fermentation of Coffee Pulp Wastes [PDF]

open access: yesJurnal Biodjati, 2019
An α-L-Rhamnosidase released by Aspergillus niger during solid-state fermentation (SSF) using coffee pulp (CP) wastes media has been investigated. The activity of α-L-Rhamnosidase based on reducing sugar production against 2% CP alkali extract substrate ...
Kahar Muzakhar, Rudju Winarsa
doaj   +5 more sources

Safety evaluation of the food enzyme α‐l‐rhamnosidase from the non‐genetically modified Penicillium adametzii strain AE‐HP [PDF]

open access: yesEFSA Journal, 2023
The food enzyme α‐l‐rhamnosidase (α‐l‐rhamnoside rhamnohydrolase; EC 3.2.1.40) is produced with the non‐genetically modified Penicillium adametzii strain AE‐HP by Amano Enzymes Inc.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +25 more
doaj   +2 more sources

Computer-Aided Design of α-L-Rhamnosidase to Increase the Synthesis Efficiency of Icariside I [PDF]

open access: yesFrontiers in Bioengineering and Biotechnology, 2022
Icariside I, the glycosylation product of icaritin, is a novel effective anti-cancer agent with immunological anti-tumor activity. However, very limited natural icariside I content hinders its direct extraction from plants.
Jia-Jun Huang   +7 more
doaj   +2 more sources

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