Details

Autor(en) / Beteiligte

• Nakada, Tetsuya
• Maruta, Kazuhiko
• Tsusaki, Keiji
• Kubota, Michio
• Chaen, Hiroto
• Sugimoto, Toshiyuki
• Kurimoto, Masashi
• Tsujisaka, Yoshio

Titel

Purification and Properties of a Novel Enzyme, Maltooligosyl Trehalose Synthase, from Arthrobacter sp. Q36

Ist Teil von

• Bioscience, biotechnology, and biochemistry, 1995-12, Vol.59 (12), p.2210-2214

Ort / Verlag

Tokyo: Taylor & Francis

Erscheinungsjahr

1995

Quelle

MEDLINE

Beschreibungen/Notizen

• Arthrobacter sp. Q36 produces a novel enzyme, maltooligosyl trehalose synthase, which catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (α-maltooligosyl α-D-glucoside) by intramolecular transglycosylation. The enzyme was purified from a cell-free extract to an electrophoretically homogeneous state by successive column chromatography on Sepabeads FP-DA13, DEAE-Sephadex A-50, Ultrogel AcA44, and Butyl-Toyopearl 650M. The enzyme was specific for maltooligosaccharides except maltose, and catalyzed the conversion to form maltooligosyl trehalose. The K m of the enzyme for maltotetraose, maltopentaose, maltohexaose, and maltoheptaose were 22.9mM, 8.7mM, 1.4mM, and 0.9mM, respectively. The enzyme had a molecular mass of 81,000 by SDS-polyacrylamide gel electrophoresis and a pI of 4.1 by gel isoelectrofocusing. The N-terminal and C-terminal amino acids of the enzyme were methionine and serine, respectively. The enzyme showed the highest activity at pH 7.0 and 40°C, and was stable from pH 6.0 to 9.5 and up to 40°C. The enzyme activity was inhibited by Hg 2+ and Cu2 + .