EC Number   |
Application |
Reference |
|---|
   3.2.1.40 | biotechnology |
enzyme efficiently releases monoterpenols from an aroma precursor from muscat grape juice |
654992 |
| 3.2.1.40 | biotechnology |
potential use as a biocatalyst for diverse biotechnological applications |
751348 |
| 3.2.1.40 | 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 |
715726 |
| 3.2.1.40 | drug development |
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 |
-, 750829 |
| 3.2.1.40 | food industry |
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 |
751161 |
| 3.2.1.40 | 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 |
751340 |
| 3.2.1.40 | 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) |
-, 750855 |
| 3.2.1.40 | 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 |
-, 750829 |
| 3.2.1.40 | 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 |
-, 750899 |
| 3.2.1.40 | 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 |
-, 750586 |
