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 journalArticlepeer-review

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

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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