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Literature summary for 3.2.1.40 extracted from

  • Lei, L.; Huang, B.; Liu, A.; Lu, Y.; Zhou, J.; Zhang, J.; Wong, W.
    Enzymatic production of natural sweetener trilobatin from citrus flavanone naringin using immobilised alpha-L-rhamnosidase as the catalyst (2018), Int. J. Food Sci. Technol., 53, 2097-2103 .
No PubMed abstract available

Application

Application Comment Organism
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) Aspergillus niger

General Stability

General Stability Organism
enzyme immobilised onto kappa-carrageenan beads surface can be recycled for 10 reactions, 90% yield retained Aspergillus niger

Inhibitors

Inhibitors Comment Organism Structure
acetone the addition of organic solvent can enhance solubility of naringin dihydrochalcone, but it also decreases enzyme activity. Dimethyl sulfoxide, acetone and methanol decrease enzyme activity more seriously than that of ethanol. When necessary, ethanol as a co-solvent with quantity less than 5% (v/v) is ecommended to improve the hydrolysis reaction of naringin dihydrochalcone Aspergillus niger
dimethyl sulfoxide the addition of organic solvent can enhance solubility of naringin dihydrochalcone, but it also decreases enzyme activity. Dimethyl sulfoxide, acetone and methanol decrease enzyme activity more seriously than that of ethanol. When necessary, ethanol as a co-solvent with quantity less than 5% (v/v) is ecommended to improve the hydrolysis reaction of naringin dihydrochalcone Aspergillus niger
methanol the addition of organic solvent can enhance solubility of naringin dihydrochalcone, but it also decreases enzyme activity. Dimethyl sulfoxide, acetone and methanol decrease enzyme activity more seriously than that of ethanol. When necessary, ethanol as a co-solvent with quantity less than 5% (v/v) is recommended to improve the hydrolysis reaction of naringin dihydrochalcone Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger R9W5L0
-
-
Aspergillus niger JMU-TS528 R9W5L0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
naringin dihydrochalcone + H2O
-
Aspergillus niger trilobatin + alpha-L-rhamnose
-
?
naringin dihydrochalcone + H2O
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Aspergillus niger JMU-TS528 trilobatin + alpha-L-rhamnose
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
immobilized enzyme Aspergillus niger

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 70 55°C: about 50% of maximal activity, 70°C: about 40% of maximal activity, immobilized enzyme Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
significantly inactivated at the temperature above 65°C Aspergillus niger

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6
-
Aspergillus niger

pH Range

pH Minimum pH Maximum Comment Organism
4 8 when the enzyme is in the condition of pH 4.0 to 5.0 or pH 7.0 to 8.0, its activity decreases dramatically to 40% yield or even less, soluble enzyme Aspergillus niger