L-Rhamnose induction of
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]
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]
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]
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]
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]
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]
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]
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]
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]
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

