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

Kousuke Moriyama; Kyunga Sung; Masahiro Goto; Noriho Kamiya

doi:10.1016/j.jbiosc.2011.02.002

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

Kousuke Moriyama, Kyunga Sung, Masahiro Goto, Noriho Kamiya

Applied Chemistry

Research output: Contribution to journal › Article › peer-review

27 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	650-653
Number of pages	4
Journal	Journal of Bioscience and Bioengineering
Volume	111
Issue number	6
DOIs	https://doi.org/10.1016/j.jbiosc.2011.02.002
Publication status	Published - Jun 2011

All Science Journal Classification (ASJC) codes

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1016/j.jbiosc.2011.02.002

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

abstract = "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.",

author = "Kousuke Moriyama and Kyunga Sung and Masahiro Goto and Noriho Kamiya",

note = "Funding Information: We are grateful to Ajinomoto Co., Inc. (Japan) for providing MTG samples. This work was supported by a Grant-in-Aid for the Global COE program “Science for Future Molecular Systems”, from the Ministry of Education, Culture, Sports, Science and Technology of Japan .",

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AU - Moriyama, Kousuke

AU - Sung, Kyunga

AU - Goto, Masahiro

AU - Kamiya, Noriho

N1 - Funding Information: We are grateful to Ajinomoto Co., Inc. (Japan) for providing MTG samples. This work was supported by a Grant-in-Aid for the Global COE program “Science for Future Molecular Systems”, from the Ministry of Education, Culture, Sports, Science and Technology of Japan .

PY - 2011/6

Y1 - 2011/6

N2 - 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.

AB - 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.

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

Abstract

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