Horse liver alcohol dehydrogenase immobilized on inorganic supports: Stabilizing effect of bound protein

Johnson, Donna

doi:10.1002/bit.260200714

Cited by 15 publications

(2 citation statements)

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“…1 The immobilization of ADH onto numerous supports was reported in the literature. [2][3][4][5] ADH from yeast and horse liver has been coupled to natural 6,7 and synthetic 8 carriers. Many studies have been reported on the stability of immobilized ADH toward heat, 9 continuous operation, 10 storage, 11 and different substrates.…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of yeast alcohol dehydrogenase by entrapment and covalent binding to polymeric supports

Soni

Desai

Devi

2001

J of Applied Polymer Sci

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Yeast alcohol dehydrogenase (YADH), which catalyzes oxidoreductions of a broad spectrum of substrates, was immobilized by entrapping it into a network of a poly(acrylamide-co-hydroxyethyl methacrylate) copolymer and was also covalently bound onto porous chitosan beads activated through glutaraldehyde. Maximum retention of YADH activity achieved was 90 and 24% for entrapment and covalent binding, respectively. The results obtained for thermal, storage, and operational stability of entrapped and covalently bound YADH were compared with free YADH. The immobilized enzyme showed improved thermal and storage stability. The immobilized enzymes also retained 50% activity after six and eight cycles. Enzyme-catalyzed oxidation of ethanol was observed to be diffusion-controlled through Lineweaver-Burk plots.

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Section: Introductionmentioning

confidence: 99%

“…Alcohol dehydrogenase (ADH), a complex redox enzyme, contains four subunits bound to zinc and a sensitive sulfhydryl group essential for its activity 1. The immobilization of ADH onto numerous supports was reported in the literature 2–5. ADH from yeast and horse liver has been coupled to natural6, 7 and synthetic8 carriers.…”

Section: Introductionmentioning

confidence: 99%