PMID: 2112366Mar 1, 1990Paper

Immobilization of amyloglucosidase using two forms of polyurethane polymer

Applied Biochemistry and Biotechnology
K B StoreyA C Chakrabarti

Abstract

Amyloglucosidase was covalently immobilized using two hydrophilic prepolymers: Hypol FHP 2002 (creates foams) and Hypol FHP 8190H (creates gels). The foamable prepolymer was superior as a support for enzyme immobilization. The percent activity immobilized in the polyurethane foams was 25 +/- 1.5%. Large substrates (greater than 200,000 daltons in mol wt) were hydrolyzed as effectively as smaller ones by the immobilized enzyme. The Km value of the foam-immobilized enzyme increased from 0.76 mg/mL (free) to 0.86 mg/mL (immobilized), whereas the Vmax dropped from 90.9 (free) to 12.4 nmol glucose/min/mL (immobilized). The long-term (2 mo) storage stability of amyloglucosidase was enhanced by immobilization in foams (70% activity retained; free enzyme only retained 50%). Immobilization also improved the enzyme stability to various denaturing agents (sodium chloride, urea, and ethanol). The immobilized enzyme exhibited increased stability compared to the free enzyme at high temperatures (95 degrees C). Both glycogen and starch could be utilized by the immobilized enzyme, indicating that this technique could prove useful for starch hydrolysis.

References

Dec 5, 1987·Biotechnology and Bioengineering·A WójcikJ Fiedurek

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Citations

Aug 20, 1996·Biotechnology and Bioengineering·K E Lejeune, A J Russell
Jan 1, 1992·Applied Biochemistry and Biotechnology·D Y Schafhauser, K B Storey
May 19, 2000·Biomaterials·J L PanzaA J Russell
Aug 6, 2004·Journal of Environmental Management·M S Alhakawati, C J Banks
Sep 19, 2000·Biotechnology and Bioengineering·M BakkerR A Sheldon
Jan 1, 1992·Journal of Biomaterials Science. Polymer Edition·M J DanilichR E Marchant
Feb 3, 1999·Annals of the New York Academy of Sciences·K E LeJeuneA J Russell
Apr 20, 1997·Biotechnology and Bioengineering·K E LeJeuneA J Russell

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