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Immobilization of oxyreductases on inorganic supports based on alumina. Immobilization of lactate dehydrogenase on alumina by adsorption
Author(s) -
Kovalenko G. A.,
Shitova N. B.,
Sokolovskii V. D.
Publication year - 1981
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260230805
Subject(s) - adsorption , lactate dehydrogenase , chemistry , dehydrogenase , catalysis , enzyme , immobilized enzyme , molecule , chromatography , inorganic chemistry , organic chemistry
Lactate dehydrogenase (LDH) was adsorbed on low‐(γ, η) and high ‐(θ, α) temperature forms of alumina. θ‐Al 2 O 3 exhibited the greatest adsorption ability. The maximum adsorption value was 30 mg LDH/g of a carrier. The conditions for irreversible adsorption have been determined. An adsorption isotherm on θ‐Al 2 O 3 for pH 6.0 has been obtained; the LDH ads surface area and the carrier surface portion accessible to the enzyme molecules have been calculated. The reaction kinetic parameter were determined by taking into account the reaction proceeding in the intradiffusional region. The specific catalytic activity ( A spec ) of LDH ads at small surface coverage of θ‐Al 2 O 3 is five times less than A spec of the native enzyme and K M imm with respect to NADH exceeds K M nat by two orders or magnitude. The is evidence for a strong LDH–Al 2 O 3 interaction and a considerable deformation of the enzyme globule. A spec and K M decrease as the amount of the enzyme attached to the carrier increases. Due to adsorption. LDH becomes thermostable and durable. The LDH ads samples conserve 20–40% of their activity at room temperature during a year.