PubMed HealthSearch

PubMed · 119963

[Immobilization of commercial glucoamylase on the polymer carrier].

Abstract

Commercial glucoamylase was immobilized on the polymer carrier produced by the binding of 4--8 mol.% 4,4'-diamine diphenyl oxide of the maleic anhydride copolymer with N-vinyl pyrrolidone. Two types of immobilized preparations were obtained: with covalent absorption and covalent attachment of the enzyme to the polymer. Glucoamylase activity of the first preparation was 20,000--60,000 and that of the second was 40--120 units/g polymer. Covalent-attached preparations showed a more prolonged action than covalent-absorbed ones.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

V L Iarovenko, T N Pisarenko, B A Ustinnikov, V I Rodzevich, N A Camoilova. [Immobilization of commercial glucoamylase on the polymer carrier].. https://pubmed.ncbi.nlm.nih.gov/119963/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Hydrolysis of organophosphate insecticides by an immobilized-enzyme system.

An enzyme preparation that could detoxify parathion and eight other organophosphate pesticides was covalently bound to either porous glass or porous silica beads. This immobilized-enzyme system was examined for its use in detoxification of pesticides in production wastewaters. The kinetics of parathion hydrolysis were examined at flow rates up to 96 liter/hr and at influent substrate concentrations ranging from 10--250 mg/liter. The enzyme reactor was able to hydrolyze 95% or more of the parathion added to industrial wastewaters generated during its production, thus reducing the effluent parathion concentration to below 500 ppb. Laboratory continuous-flow experiments were conducted for 70 days with industrial wastewater and indicated no loss in immobilized-enzyme activity. The influence of pH, temperature, solvents, and detergents on enzyme stability and activity and enzyme reactor kinetics will be discussed.

Enzymes, Immobilized

Properties and uses of immobilized light-emitting enzyme systems from Beneckea harveyi.

Bacterial luciferase and NADH:FMN oxidoreductase have been immobilized onto arylamine glass beads. These immobilized enzymes can detect as little as 0.2 pmol of NADH per assay sample. Glucose-6-phosphate dehydrogenase has been co-immobilized with these enzymes, and with this system it is possible to quantitate 1 pmol of glucose 6-phosphate. By co-immobilizing a fourth enzyme, hexokinase, onto the glass beads, the system can reproducibly detect 20 pmol of glucose per liter. These immobilized enzyme systems are potentially superior to soluble enzymes by being reusable and much more stable. We compared the light-emitting properties of the immobilized enzyme systems with that of an equivalent mixture of the soluble enzymes. The most striking difference was the apparently more efficient conversion of NADH or glucose 6-phosphate to light by the immobilized enzymes. We used hydroxysteroid dehydrogenase in developing a soluble coupled system for the assay of androsterone and testosterone. The lower limit of detection was 100 pmol.

Enzymes, Immobilized