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Literature summary for 3.1.3.2 extracted from

  • Srivastava, P.K.; Anand, A.
    Immobilization of acid phosphatase from Vigna aconitifolia seeds on chitosan beads and its characterization (2014), Int. J. Biol. Macromol., 64, 150-154.
    View publication on PubMed

Application

Application Comment Organism
synthesis immobilization of enzyme onto glutaraldehyde activated chitosan beads. Chitosan beads activated with 2% of glutaraldehyde demonstrate maximum immobilization yield of about 83%. The immobilized enzyme shows optimum activity at pH 7.0, while the soluble form is maximally active at pH 5.0. Both soluble and immobilized acid phosphatase exhibit maximum activity at 60°C. The immobilization on chitosan beads enhances the shelf life of acid phosphatase. The immobilized enzyme retains its more than 50% hydrolytic activity for approximately two months and can be reused for more than 40 cycles of reaction Vigna aconitifolia

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.37
-
4-nitrophenyl phosphate pH 5.0, 37°C, enzyme immobilized onto chitosan beads Vigna aconitifolia

Organism

Organism UniProt Comment Textmining
Vigna aconitifolia
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
Vigna aconitifolia
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate
-
Vigna aconitifolia 4-nitrophenol + phosphate
-
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