Results 11 to 20 of about 1,494 (149)

Efficient production of icariin and baohuoside I from Epimedium Folium flavonoids by fungal α- l -rhamnosidase hydrolysing regioselectively the terminal rhamnose of epimedin C [PDF]

open access: yesBiotechnology for Biofuels and Bioproducts, 2023
Industrial application of icariin and baohuoside I has been hindered by the short supply to a great extent. In this work, a novel GH78 α- l-rhamnosidase AmRha catalyzed the bioconversion of low-value epimedin C in crude Epimedium Folium flavonoids (EFs ...
Shanshan Zhang   +5 more
doaj   +2 more sources

Characterization of a Thermophilic and Acidophilic GH78 α-L-Rhamnosidase from Thermotoga sp. 2812B Capable of Efficiently Hydrolyzing a Variety of Natural Flavonoid Diglycosides [PDF]

open access: yesBiomolecules
α-L-Rhamnosidase can specifically hydrolyze plant natural glycosides and holds significant potential for biocatalytic applications in functional foods, healthy products, and pharmaceutical industries.
Bin-Chun Li   +5 more
doaj   +2 more sources

Biotechnological and bio-industrial applications of alpha–l-rhamnosidase enzyme [PDF]

open access: yesRevista Politécnica
α -L-rhamnosidase is an important biotechnology enzyme that is used in various foods, chemicals and pharmaceutical industries. The α-L-rhamnosidases (α- RHA) belong to a group of glycosyl hydrolases having biotechnological potential in the proesses ...
Arshad Muhammad   +3 more
doaj   +3 more sources

Upscale of recombinant α-L-rhamnosidase production by Pichia pastoris MutS strain [PDF]

open access: yesFrontiers in Microbiology, 2015
Pichia pastoris is currently one of the most preferred microorganisms for recombinant enzyme production due to its efficient expression system. The advantages include the production of high amounts of recombinant proteins containing the appropriate ...
Kristína eMarkošová   +4 more
doaj   +2 more sources

A Novel Ginsenoside-Transforming α-L-Rhamnosidase from Bifidobacterium: Screening, Characterization and Application [PDF]

open access: yesBiomolecules
Despite the rapid advancement of glycosidase biotechnology, ginsenoside-transforming rhamnosidases remain underexplored due to a lack of research. In this study, we aimed to bridge this gap by evaluating eight putative rhamnosidases for their ability to ...
Chang-Hao Cui   +3 more
doaj   +2 more sources

An Organic Solvent-Tolerant α-L-Rhamnosidase from Dictyoglomus thermophilum and Its Application in Production of Icariside I from Icariin [PDF]

open access: yesMolecules
Icariside I, a bioactive flavonoid derivative derived from Herba epimedii, demonstrates better pharmacological properties compared to its precursor icariin.
Jinyue Hu   +5 more
doaj   +2 more sources

Gap Analysis of Metabolic Conversions of Off-Flavors and Antinutrients in Plant-Based Substrates. [PDF]

open access: yesCompr Rev Food Sci Food Saf
ABSTRACT To drastically reduce the carbon footprint of the food production chain, a major shift towards alternatives to conventional meat and dairy products is required. The use of plant‐based proteins is a promising route, but it also comes with challenges: Plant‐based proteins often contain antinutritional factors and off‐flavors, which can ...
Kuijpers RI   +16 more
europepmc   +2 more sources

Enhanced Antioxidant and Anti-Inflammatory Activities of Diospyros lotus Leaf Extract via Enzymatic Conversion of Rutin to Isoquercitrin [PDF]

open access: yesAntioxidants
Isoquercitrin, a monoglucoside form of quercetin, exhibits superior antioxidant, anti-inflammatory, and cardiovascular protective effects in comparison to its precursor, rutin. However, its natural abundance is limited.
Yeong-Su Kim   +2 more
doaj   +2 more sources

Highly efficient bioconversion of icariin to icaritin by whole-cell catalysis [PDF]

open access: yesMicrobial Cell Factories, 2023
Background Icaritin is an aglycone of flavonoid glycosides from Herba Epimedii. It has good performance in the treatment of hepatocellular carcinoma in clinical trials. However, the natural icaritin content of Herba Epimedii is very low.
Yu Lin   +8 more
doaj   +2 more sources

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

open access: yesEFSA Journal
The food enzyme α‐l‐rhamnosidase (α‐l‐rhamnoside rhamnohydrolase; EC 3.2.1.40) is produced with Penicillium adametzii strain AE‐HP by Amano Enzymes Inc.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +21 more
doaj   +2 more sources

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