TY - JOUR
T1 - Enzymatic modification of β-lactoglobulin with N-fatty-acyl-dipeptide by transglutaminase from Streptomyces mobaraense
AU - Wada, Eiko
AU - Masuda, Haruki
AU - Imamura, Koreyoshi
AU - Sakiyama, Takaharu
AU - Adachi, Shuji
AU - Matsuno, Ryuichi
AU - Nakanishi, Kazuhiro
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
KW - Enzymatic modification
KW - Fatty acid
KW - Transglutaminase
KW - β-lactoglobulin
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U2 - 10.1023/A:1011699921628
DO - 10.1023/A:1011699921628
M3 - Article
AN - SCOPUS:0034807203
SN - 0141-5492
VL - 23
SP - 1367
EP - 1372
JO - Biotechnology Letters
JF - Biotechnology Letters
IS - 17
ER -