Immobilization of alkaline phosphatase on magnetic particles by site-specific and covalent cross-linking catalyzed by microbial transglutaminase

Bacterial alkaline phosphatase (BAP) was site-specifically and covalently immobilized on magnetic particles (MPs) using the enzymatic reaction of microbial transglutaminase (MTG). Immobilization efficiency was affected by the chemical surface treatment of MPs and immobilized BAP exhibited more than...

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Veröffentlicht in:	Journal of bioscience and bioengineering 2011-06, Vol.111 (6), p.650-653
Hauptverfasser:	Moriyama, Kousuke, Sung, Kyunga, Goto, Masahiro, Kamiya, Noriho
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkaline phosphatase Alkaline Phosphatase - chemistry Bacterial Proteins - chemistry Catalysis crosslinking enzymatic reactions Enzymes, Immobilized - chemistry Escherichia coli - enzymology Magnetic particles Magnetics Microbial transglutaminase protein-glutamine gamma-glutamyltransferase recycling Site-specific and covalent immobilization Substrate Specificity Transglutaminases - chemistry
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Beschreibung
Zusammenfassung:	Bacterial alkaline phosphatase (BAP) was site-specifically and covalently immobilized on magnetic particles (MPs) using the enzymatic reaction of microbial transglutaminase (MTG). Immobilization efficiency was affected by the chemical surface treatment of MPs and immobilized BAP exhibited more than 90% of the initial activity after 10 rounds of recycling.
ISSN:	1389-1723 1347-4421
DOI:	10.1016/j.jbiosc.2011.02.002