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Literature summary for 2.7.1.30 extracted from

  • Aggarwal, V.; Pundir, C.S.
    Rational design of nanoparticle platforms for cutting-the-fat covalent immobilization of lipase, glycerol kinase, and glycerol-3-phosphate oxidase on metal nanoparticles (2016), Methods Enzymol., 571, 197-223 .
    View publication on PubMed
Search for more literature for 2.7.1.30

Protein Variants

Protein Variants Comment Organism
additional information rational design of nanoparticle platforms for cutting-the-fat, covalent immobilization of lipase, glycerol kinase, and glycerol-3-phosphate oxidase on metal nanoparticles. Co-immobilization of enzymes onto nanoparticles aggregates is expected to produce faster kinetics than their individual immobilizations on separate matrices. The combined activities of co-immobilized enzymes are tested amperometrically, and these composite nanobiocatalysts show optimum activity within 4-5 s, at pH 6.5-7.5 and 35°C, when polarized at a potential between 0.1 and 0.4 V. Co-immobilized enzymes show excellent linearity within 50-700 mg/dl of the lipid with detection limit of 20 mg/dl for triolein. The half life of co-immobilized enzymes is 7 months, when stored dry at 4°C, which is very convenient for practical applications. Co-immobilized biocatalysts measured triglycerides (TGs) in the sera of apparently healthy persons and persons suffering from hypertriglyceridemia, which is recognized as a leading cause for heart disease. The measurement of serum TG by co-immobilized enzymes is unaffected by the presence of a number of serum substances, tested as potential interferences. Attachment of enzymes onto an insoluble support not only provides their reusability but also realizes the extra stabilization rendered by the multipoint covalent attachment or multisubunit binding of the enzymes on solid supports. Use of rationally designed nanoscaffolds for enzyme binding, method development, evaluation, and optimization, overview Cellulomonas sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Cellulomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
128000
-
 gel filtration Cellulomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + glycerol Cellulomonas sp.
-
 ADP + sn-glycerol 3-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Cellulomonas sp.
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Cellulomonas sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
25 75 purified enzyme, pH 9.8, 25°C Cellulomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glycerol
-
 Cellulomonas sp. ADP + sn-glycerol 3-phosphate
-
 ?
additional information combined assay of lipase, glycerol kinase, and glycerol-3-phosphate oxidase immobilized onto nanoparticles aggregates as part of a biosensot electrode (onto nanocomposite of ZnONPs/chitosan electrodeposited onto Pt electrode) Cellulomonas sp. ?
-
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 enzyme in biosensor on graphite electrode Cellulomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 enzyme in biosensor on graphite electrode Cellulomonas sp.

General Information

General Information Comment Organism
metabolism lipase, glycerol kinase, and glycerol-3-phosphate oxidase are required for lipid analysis in a cascade reaction Cellulomonas sp.