3.2.1.40: alpha-L-rhamnosidase
This is an abbreviated version!
For detailed information about alpha-L-rhamnosidase, go to the full flat file.
Word Map on EC 3.2.1.40
-
3.2.1.40
-
l-rhamnose
-
decumbens
-
debittering
-
hesperidin
-
prunin
-
grapefruit
-
albidus
-
food industry
-
erubescens
-
eupenicillium
-
rhamnosylated
-
hesperidinase
-
beta-d-glucosidase
-
nutrition
-
alpha-1,2
-
gellan
-
synthesis
-
biotechnology
-
industry
-
drug development
-
degradation
-
pharmacology
- 3.2.1.40
- l-rhamnose
- decumbens
-
debittering
- hesperidin
- prunin
- grapefruit
- albidus
- food industry
- erubescens
- eupenicillium
-
rhamnosylated
-
hesperidinase
- beta-d-glucosidase
- nutrition
-
alpha-1,2
- gellan
- synthesis
- biotechnology
- industry
- drug development
- degradation
- pharmacology
Reaction
Synonyms
alpha-L-rhamnosidase, alpha-L-rhamnosidase A, alpha-L-rhamnosidase B, alpha-L-rhamnosidase N, alpha-L-rhamnosidase Ram A, alpha-L-rhamnosidase T, alpha-RHA, AoRha, AorhaA, BtRha, BtRha78A, DtRha, EC 3.2.1.66, GH106 alpha-L-rhamnosidase, gypenoside-alpha-L-rhamnosidase, KoRha, L-rhamnosidase, More, naringinase, pnp-rhamnohydrolase, RamA, RHA-P, RhaA, RhaB, RhaB1, RhaB2, RhaL1, Rham, rhamnosidase, alpha -L-, RhmA, saponin-alpha-L-rhamnosidase
ECTree
Advanced search results
Application
Application on EC 3.2.1.40 - alpha-L-rhamnosidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
biotechnology
degradation
recombinant rhamnosidase is thermostable and highly active for naringin hydrolysis up to more than 77%, thus producing L-rhamnose and prunin from citrus peel waste
drug development
food industry
industry
nutrition
pharmacology
alpha-L-rhamnosidase is an important enzyme with applications in the pharmaceutical industries because it can release terminal L-rhamnose residues from various natural products. The D594Q and G827K/D594Q mutant enzymes are more suitable for the industrial processes of isoquercitrin preparation than the wild-type enzyme
synthesis
-
enzyme efficiently releases monoterpenols from an aroma precursor from muscat grape juice
biotechnology
potential use as a biocatalyst for diverse biotechnological applications
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications
drug development
Aspergillus niger JMU-TS528
-
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications
-
alpha-L-rhamnosidase is an important enzyme with applications in the food industries because it can release terminal L-rhamnose residues from various natural products. The D594Q and G827K/D594Q mutant enzymes are more suitable for the industrial processes of isoquercitrin preparation than the wild-type enzyme
food industry
Aspergillus terreus alpha-L-rhamnosidase specifically hydrolyses the glycosidic linkage of dulcoside A (the bitterest compounds in steviol glycoside mixtures), and converts it to rubusoside. During a 12 h biotransformation, the dulcoside A from crude leaf extracts is completely converted by recombinant alpha-L-rhamnosidase from Aspergillus terreus into rubusoside. This process offers a promising approach for reducing the bitterness of steviol glycoside mixtures
food industry
efficient and cost-effective enzymatic production method for preparation of the high-valued natural sweetener trilobatin is developed by the combination of hydrogenation and enzymatic hydrolysis reactions with alpha-L-rhamnosidase as the catalyst in aqueous medium. This technology is adopting the cheap and largely available citrus flavanone naringin as the starting material for trilobatin synthesis, and the present enzymatic technology is possibly utilised by commercial for scale-up production. The production is a straightforward two-step process, in which naringin is hydrogenated into naringin dihydrochalcone and followed by removal of the rhamnosyl group of naringin dihydrochalcone by enzymatic hydrolysis using immobilised alpha-L-rhamnosidase as the catalyst. Under optimised conditions, an overall yield of 96% is achieved with a very low loading of alpha-L-rhamnosidase catalyst at 60 °C in a neutral aqueous buffer solution within 2 h. The immobilised alpha-L-rhamnosidase catalyst can be recycled for 10 reactions (90% yield retained)
food industry
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications
food industry
the enzyme can efficiently remove naringin from pomelo juice without changing its aroma. It is desirable for debittering citrus juice thereby improving the quality of juice
food industry
the enzyme can remove the bitter taste of naringin from citrus juices. Improvement of thermostabilty can promote the practical value of the enzyme in citrus juice processing
food industry
-
the enzyme exhibits transglycosylating activity, which can synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. The enzyme has potential value for glycoside synthesis in the food industry
food industry
-
the enzyme is used to enhance wine aromas or to debitter citrus juices by releasing L-rhamnose
food industry
-
the purified enzyme has potential for enhancement of wine aroma
food industry
with the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry
food industry
Aspergillus niger JMU-TS528
-
the enzyme can remove the bitter taste of naringin from citrus juices. Improvement of thermostabilty can promote the practical value of the enzyme in citrus juice processing
-
food industry
Aspergillus niger JMU-TS528
-
with the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry
-
food industry
Aspergillus niger JMU-TS528
-
the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications
-
food industry
Aspergillus niger JMU-TS528
-
efficient and cost-effective enzymatic production method for preparation of the high-valued natural sweetener trilobatin is developed by the combination of hydrogenation and enzymatic hydrolysis reactions with alpha-L-rhamnosidase as the catalyst in aqueous medium. This technology is adopting the cheap and largely available citrus flavanone naringin as the starting material for trilobatin synthesis, and the present enzymatic technology is possibly utilised by commercial for scale-up production. The production is a straightforward two-step process, in which naringin is hydrogenated into naringin dihydrochalcone and followed by removal of the rhamnosyl group of naringin dihydrochalcone by enzymatic hydrolysis using immobilised alpha-L-rhamnosidase as the catalyst. Under optimised conditions, an overall yield of 96% is achieved with a very low loading of alpha-L-rhamnosidase catalyst at 60 °C in a neutral aqueous buffer solution within 2 h. The immobilised alpha-L-rhamnosidase catalyst can be recycled for 10 reactions (90% yield retained)
-
food industry
Aspergillus tubingensis JMU-TS529
-
the enzyme can efficiently remove naringin from pomelo juice without changing its aroma. It is desirable for debittering citrus juice thereby improving the quality of juice
-
food industry
Alternaria alternata SK37.001
-
the enzyme is used to enhance wine aromas or to debitter citrus juices by releasing L-rhamnose
-
food industry
Aspergillus oryzae NL-1
-
the enzyme exhibits transglycosylating activity, which can synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. The enzyme has potential value for glycoside synthesis in the food industry
-
food industry
Fusarium verticillioides MTCC-2088
-
the purified enzyme has potential for enhancement of wine aroma
-
stable alpha-L-rhamnosidase with cleaving terminal alpha-L-rhamnose activity has great potential in industrial application. Enhancing the thermostability of alpha-L-rhamnosidase from Aspergillus terreus makes it a good candidate for industrial processes of isoquercitrin preparation
industry
the enzyme is a promising alternative biocatalyst for industrial applications due to good pH stability, relatively high thermostability and tolerance to low concentration of alcohols
industry
-
the enzyme is a promising alternative biocatalyst for industrial applications due to good pH stability, relatively high thermostability and tolerance to low concentration of alcohols
-
nutrition
alpha-L-rhamnosidases are used in wine production
nutrition
-
production of bioavailable flavonoid glucosides in fruit juices and green tea by use of fungal alpha-L-rhamnosidases RhaA and RhaB from Aspergillus aculeatus
nutrition
application in fruit juice and wine industry, bioreactor design for production of rhamnose from natural flavinoids such as naringin
nutrition
-
production of bioavailable flavonoid glucosides in fruit juices and green tea by use of fungal alpha-L-rhamnosidases RhaA and RhaB from Aspergillus aculeatus
-
synthesis
immobilization of recombinant enzyme on Ca2+ alginate beads. Immobilization enables its reutilization up to 9 hydrolysis batches without an appreciable loss in activity
synthesis
-
a wild-type alpha-L-rhamnosidase from Alternaria sp. L1 can synthesize rhamnose-containing chemicals through reverse hydrolysis reaction with inexpensive rhamnose as glycosyl donor
synthesis
adding sorbitol has great potential to promote enzymatic conversion of rutin to isoquercitrin production. Isoquercitrin has several biological activities, including anti-mutagenesis, anti-virus, anti-hypertensive, anti-proliferative effects, lipid peroxidation, oxidative-stress protection as well as other pharmacological effects