Enzymatic modification of β-lactoglobulin with N-fatty-acyl-dipeptide by transglutaminase from Streptomyces mobaraense

Eiko Wada, Haruki Masuda, Koreyoshi Imamura, Takaharu Sakiyama, Shuji Adachi, Ryuichi Matsuno, Kazuhiro Nakanishi

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

β-Lactoglobulin was enzymatically acylated with N-lauroyl-L-glutaminyl-glycine and N-lauroyl-L-glutamyl-L-lysine using transglutaminase from Streptomyces mobaraense. The modification of the protein with N-fatty-acyl-dipeptide was confirmed by SDS-PAGE, gel chromatography, HPLC, amino acid analysis, and TOF-MS. The degrees of the protein modification with N-lauroyl-L-glutaminyl-glycine and N-lauroyl-L-glutamyl-L-lysine were estimated to be 2-4 and 1.5 residues per molecule, respectively.

Original languageEnglish
Pages (from-to)1367-1372
Number of pages6
JournalBiotechnology Letters
Volume23
Issue number17
DOIs
Publication statusPublished - Oct 10 2001

Keywords

  • Enzymatic modification
  • Fatty acid
  • Transglutaminase
  • β-lactoglobulin

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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