A chemically modified glass surface that facilitates transglutaminase- mediated protein immobilization

Yusuke Tanaka, Satoshi Doi, Noriho Kamiya, Noriyuki Kawata, Shinji Kamiya, Kenichi Nakama, Masahiro Goto

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

An amino-modified glass surface for enzymatic protein immobilization by microbial transglutaminase (MTG) was developed. Diamine substrates with secondary amino groups in the linker moiety, like triethylenetetramine (TETA), exhibited at most a 2-fold higher reactivity in the MTG-catalyzed reaction compared to those with the alkyl linker. A 96-well glass plate was subsequently modified with selected diamine substrates. Validation of the modified surface by enzymatic immobilization of enhanced green fluorescent protein tagged with a glutamine donor-substrate peptide (LLQG) of MTG revealed that the protein loading onto the TETA-modified glass surface was approximately 15-fold higher than that on the unmodified one.

Original languageEnglish
Pages (from-to)1025-1029
Number of pages5
JournalBiotechnology letters
Volume30
Issue number6
DOIs
Publication statusPublished - Jun 1 2008

Fingerprint

Transglutaminases
Immobilization
Trientine
Glass
Diamines
Proteins
Substrates
Glutamine
Peptides
Membrane Proteins

All Science Journal Classification (ASJC) codes

  • Biotechnology

Cite this

A chemically modified glass surface that facilitates transglutaminase- mediated protein immobilization. / Tanaka, Yusuke; Doi, Satoshi; Kamiya, Noriho; Kawata, Noriyuki; Kamiya, Shinji; Nakama, Kenichi; Goto, Masahiro.

In: Biotechnology letters, Vol. 30, No. 6, 01.06.2008, p. 1025-1029.

Research output: Contribution to journalArticle

Tanaka, Yusuke ; Doi, Satoshi ; Kamiya, Noriho ; Kawata, Noriyuki ; Kamiya, Shinji ; Nakama, Kenichi ; Goto, Masahiro. / A chemically modified glass surface that facilitates transglutaminase- mediated protein immobilization. In: Biotechnology letters. 2008 ; Vol. 30, No. 6. pp. 1025-1029.
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