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Title: Structurally stable gel bead containing entrapped enzyme and method for manufacture thereof

Abstract

A structurally stable gel bead containing an entrapped enzyme and a method for its manufacture. The enzyme is covalently cross-linked to gelatin in the presence of glutaraldehyde prior to the formation of the gel bead, to prevent leakage of the enzyme. Propylene glycol alginate is then added to the mixture. Once the gel beads are formed, they are then soaked in glutaraldehyde, which imparts structural stability to the gel beads. This method can be used with many types of enzymes, such as proteases, carbohydrases, proteases, ligases, isomerases, oxidoreductases, and specialty enzymes. These and other enzymes can be immobilized in the gel beads and utilized in a number of enzymatic processes. Exogenously added ions are not required to maintain the structural stability of these gel beads.

Inventors:
 [1]
  1. Oak Ridge, TN
Issue Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
OSTI Identifier:
872026
Patent Number(s):
5846762
Assignee:
Lockheed Martin Energy Research Systems, Inc. (Oak Ridge, TN)
Patent Classifications (CPCs):
Y - NEW / CROSS SECTIONAL TECHNOLOGIES Y10 - TECHNICAL SUBJECTS COVERED BY FORMER USPC Y10T - TECHNICAL SUBJECTS COVERED BY FORMER US CLASSIFICATION
C - CHEMISTRY C12 - BIOCHEMISTRY C12P - FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE {
DOE Contract Number:  
AC05-84OR21400
Resource Type:
Patent
Country of Publication:
United States
Language:
English
Subject:
structurally; stable; bead; containing; entrapped; enzyme; method; manufacture; covalently; cross-linked; gelatin; presence; glutaraldehyde; prior; formation; prevent; leakage; propylene; glycol; alginate; added; mixture; beads; formed; soaked; imparts; structural; stability; types; enzymes; proteases; carbohydrases; ligases; isomerases; oxidoreductases; specialty; immobilized; utilized; enzymatic; processes; exogenously; required; maintain; propylene glycol; prevent leakage; bead containing; structurally stable; structural stability; containing entrapped; glycol alginate; entrapped enzyme; /435/264/427/428/

Citation Formats

Woodward, Jonathan. Structurally stable gel bead containing entrapped enzyme and method for manufacture thereof. United States: N. p., 1998. Web.
Woodward, Jonathan. Structurally stable gel bead containing entrapped enzyme and method for manufacture thereof. United States.
Woodward, Jonathan. Thu . "Structurally stable gel bead containing entrapped enzyme and method for manufacture thereof". United States. https://www.osti.gov/servlets/purl/872026.
@article{osti_872026,
title = {Structurally stable gel bead containing entrapped enzyme and method for manufacture thereof},
author = {Woodward, Jonathan},
abstractNote = {A structurally stable gel bead containing an entrapped enzyme and a method for its manufacture. The enzyme is covalently cross-linked to gelatin in the presence of glutaraldehyde prior to the formation of the gel bead, to prevent leakage of the enzyme. Propylene glycol alginate is then added to the mixture. Once the gel beads are formed, they are then soaked in glutaraldehyde, which imparts structural stability to the gel beads. This method can be used with many types of enzymes, such as proteases, carbohydrases, proteases, ligases, isomerases, oxidoreductases, and specialty enzymes. These and other enzymes can be immobilized in the gel beads and utilized in a number of enzymatic processes. Exogenously added ions are not required to maintain the structural stability of these gel beads.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1998},
month = {1}
}

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Works referenced in this record:

Enzymatic hydrolysis of cellulose to glucose lung immobilized ?-glucosidase
journal, March 1981


Fungal and other β-d-glucosidases — Their properties and applications
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Properties and application of immobilized ?-D-glucosidase coentrapped withZymomonas mobilis in calcium alginate
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Properties of native and immobilised preparations of β-D-glucosidase from Aspergillus niger
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Hydrolysis of cellobiose by immobilized β-glucosidase entrapped in maintenance-free gel spheres
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β-Glucosidase: microbial production and effect on enzymatic hydrolysis of cellulose
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Immobilization of Aspergillus beta-glucosidase on chitosan.
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Cellobiose hydrolysis by glutaraldehyde- treated β-glucosidase entrapped in propylene glycol alginate/bone gelatin spheres: Scientific note
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