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Immobilization of enzymes on nanoinorganic support materials: An update

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DOI: 10.1016/j.ijbiomac.2020.11.127

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Enzyme immobilization; Stability; Inorganic support nanomaterials

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Enzyme immobilization can overcome the instability and non-reusability of enzymes, improving thermal and pH stability but increasing K-m values and decreasing V-max values; Enzymes immobilized on nanoinorganic support materials show higher Delta G values and lower Delta H and Delta S values; Covalently-bound and multipoint-attached immobilization methods can reduce costs and enhance product quality compared to weak physical adsorption immobilization.
Despite the widespread use in various industries, enzyme's instability and non-reusability limit their applications which can be overcome by immobilization. The nature of the enzyme's support material and method of immobilization affect activity, stability, and kinetics properties of enzymes. Here, we report a comparative study of the effects of inorganic support materials on immobilized enzymes. Accordingly, immobilization of enzymes on nanoinorganic support materials significantly improved thermal and pH stability. Furthermore, immobilizations of enzymes on the materials mainly increased K-m values while decreased the V-max values of enzymes. Immobilized enzymes on nanoinorganic support materials showed the increase in Delta G value, and decrease in both Delta H and Delta S values. In contrast to weak physical adsorption immobilization, covalently-bound and multipoint-attached immobilized enzymes do not release from the support surface to contaminate the product and thus the cost is decreased while the product quality is increased. Nevertheless, nanomaterials can enter the environment and increase health and environmental risks and should be used cautiously. Altogether, it can be predicated that hybrid support materials, directed immobilization methods, site-directed mutagenesis, recombinant fusion protein technology, green nanomaterials and trailor-made supports will be used increasingly to produce more efficient immobilized industrial enzymes in near future. (C) 2020 Elsevier B.V. All rights reserved.

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