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Literature summary for 2.4.1.1 extracted from

  • Garg, N.; Kumar, A.
    Immobilization of starch phosphorylase from cabbage leaves: Production of glucose-1-phosphate (2008), Braz. J. Chem. Eng., 25, 229-235.
No PubMed abstract available
Search for more literature for 2.4.1.1

Application

Application Comment Organism
synthesis immobilization of partially purified enzyme using egg shell as solid support with a percentage retention of the enzyme on egg shell of nearly 56%. After immobilization, specific activity of the enzyme increases from 0. 0225 to 0.0452 with a concomitant slight alkaline shift in the optimum pH when assayed in both the directions. The immobilized enzyme also displays increased optimum temperature and thermo-stability and can be reused number of times. Use of immobilized enzyme for the production of glucose-1-phosphate Elephantopus scaber

Organism

Organism UniProt Comment Textmining
Elephantopus scaber
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Elephantopus scaber

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Elephantopus scaber
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Elephantopus scaber

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 direction of polysaccharide synthesis, half-optima at pH 5.3 and pH 7.1 Elephantopus scaber
7
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 direction of glucose 1-phosphate synthesis, half-optima at pH 6.4 and pH 7.6 Elephantopus scaber