Abstract：
:A generic approach for flavoenzyme immobilization was developed in which the flavin cofactor is used for anchoring enzymes onto the carrier. It exploits the tight binding of flavin cofactors to their target apo proteins. The method was tested for phenylacetone monooxygenase (PAMO) which is a well-studied and industrially interesting biocatalyst. Also a fusion protein was tested: PAMO fused to phosphite dehydrogenase (PTDH-PAMO). The employed flavin cofactor derivative, N6-(6-carboxyhexyl)-FAD succinimidylester (FAD*), was covalently anchored to agarose beads and served for apo enzyme immobilization by their reconstitution into holo enzymes. The thus immobilized enzymes retained their activity and remained active after several rounds of catalysis. For both tested enzymes, the generated agarose beads contained 3 U per g of dry resin. Notably, FAD-immobilized PAMO was found to be more thermostable (40% activity after 1 h at 60 °C) when compared to PAMO in solution (no activity detected after 1 h at 60 °C). The FAD-decorated agarose material could be easily recycled allowing multiple rounds of immobilization. This method allows an efficient and selective immobilization of flavoproteins via the FAD flavin cofactor onto a recyclable carrier.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Krzek M,van Beek HL,Permentier HP,Bischoff R,Fraaije MWdoi
10.1016/j.enzmictec.2015.09.006subject
Has Abstractpub_date
2016-01-01 00:00:00pages
138-143eissn
0141-0229issn
1879-0909pii
S0141-0229(15)30060-0journal_volume
82pub_type
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journal_title：Enzyme and microbial technology
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journal_title：Enzyme and microbial technology
pub_type： 杂志文章
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journal_title：Enzyme and microbial technology
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