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01742nam a2200205Ia 4500 |
| 001 |
10.1016-j.btre.2022.e00733 |
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220706s2022 CNT 000 0 und d |
| 020 |
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|a 2215017X (ISSN)
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| 245 |
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|a Sortase-mediated immobilization of Candida antarctica lipase B (CalB) on graphene oxide; comparison with chemical approach
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|b Elsevier B.V.
|c 2022
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| 856 |
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|z View Fulltext in Publisher
|u https://doi.org/10.1016/j.btre.2022.e00733
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|a In this study, Candida antarctica lipase B (CalB) was covalently immobilized on the surface of graphene oxide (GO) nanoparticles by sortase-mediated immobilization as well as a chemical attachment approach. Sortase is a transpeptidase that provides one-step purification and targeted immobilization of CalB from one specific site, presenting oriented attachment of the enzyme to a solid support. Chemical immobilization, on the other hand, is considered as a random immobilization, in which the protein can bind to the support from different regions of the protein surface. In this approach, amine-functionalized GO was further modified with glutaraldehyde to facilitate the covalent binding of CalB via its amine residues. The applied methods produced 60% and 100% immobilization yields and presented 0.106 U/mg and 0.085 U/mg of specific activities for the oriented and random immobilization, respectively. The stabilized enzyme with the sortase-mediated approach retained approximately 80% of its initial activity at 50°C. © 2022
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|a graphene oxide
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|a oriented immobilization
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|a sortase
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|a Ahmadian, G.
|e author
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|a Ahrari, F.
|e author
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|a Mohammadi, M.
|e author
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|a Moosavi, F.
|e author
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| 773 |
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|t Biotechnology Reports
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