Literature DB >> 1416951

Immobilization of glucose isomerase onto granular chicken bone.

D Y Schafhauser1, K B Storey.   

Abstract

Glucose isomerase was immobilized onto granular chicken bone (BIOBONE) by adsorption. The amount of activity bound relative to an equal amount of free enzyme was 32 +/- 1%, with the estimated specific activity decreasing from 11.1 +/- 0.7 to 3.9 +/- 0.5 U/mg protein with immobilization. Compared with the free enzyme, immobilized glucose isomerase showed a threefold increase in the Km for fructose and a fivefold decrease in Vmax. High operating temperatures were possible (greater than 55 degrees C), but continuous use and long-term storage studies showed gradual losses of activity. Both the binding and the activity of the bone-immobilized enzyme were highly resistant to treatments with detergent, ethanol, and KCl. Studies to determine mass transfer limitation effects on immobilized glucose isomerase showed that these were insignificant for this system.

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Year:  1992        PMID: 1416951     DOI: 10.1007/bf02922150

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  2 in total

1.  Immobilization of amyloglucosidase onto granular chicken bone.

Authors:  D Y Schafhauser; K B Storey
Journal:  Appl Biochem Biotechnol       Date:  1992 Jan-Mar       Impact factor: 2.926

2.  Mechanism of thermoinactivation of immobilized glucose isomerase.

Authors:  D B Volkin; A M Klibanov
Journal:  Biotechnol Bioeng       Date:  1989-04-05       Impact factor: 4.530

  2 in total

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