Publications

• Formation of trehalose from maltooligosaccharides by a novel enzymatic system.

  Maruta K., Nakada T., Kubota M., Chaen H., Sugimoto T., Kurimoto M., Tsujisaka Y.

  Biosci Biotechnol Biochem 59:1829-1834(1995) [PubMed] [EuropePMC]

• Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36.

  Nakada T., Maruta K., Tsusaki K., Kubota M., Chaen H., Sugimoto T., Kurimoto M., Tsujisaka Y.

  Arthrobacter sp. Q36 produces a novel enzyme, maltooligosyl trehalose synthase, which catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation. The enzyme was purified fro ... >> More

  Arthrobacter sp. Q36 produces a novel enzyme, maltooligosyl trehalose synthase, which catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-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 Km of the enzyme for maltotetraose, maltopentaose, maltohexaose, and maltoheptaose were 22.9 mM, 8.7 mM, 1.4 mM, and 0.9 mM, 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 degrees C, and was stable from pH 6.0 to 9.5 and up to 40 degrees C. The enzyme activity was inhibited by Hg2+ and Cu2+. << Less

  Biosci. Biotechnol. Biochem. 59:2210-2214(1995) [PubMed] [EuropePMC]

• Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius.

  Nakada T., Ikegami S., Chaen H., Kubota M., Fukuda S., Sugimoto T., Kurimoto M., Tsujisaka Y.

  A thermostable maltooligosyl trehalose synthase was purified from a cell-free extract of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius ATCC 33909 to an electrophoretically homogeneous state by successive column chromatography on Sepabeads FP-DA13, Butyl-Toyopearl 650M, DEAE-Toyop ... >> More

  A thermostable maltooligosyl trehalose synthase was purified from a cell-free extract of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius ATCC 33909 to an electrophoretically homogeneous state by successive column chromatography on Sepabeads FP-DA13, Butyl-Toyopearl 650M, DEAE-Toyopearl 650S, Ultrogel AcA44, and Mono Q. The enzyme had a molecular mass of 74,000 by SDS-polyacrylamide gel electrophoresis and a pI of 5.9 by gel isoelectrofocusing. The N-terminal amino acid of the enzyme was methionine. The enzyme showed the highest activity from pH 5.0 to 5.5 and at 75 degrees C, and was stable from pH 4.5 to 9.5 and up to 85 degrees C. The enzyme activity was inhibited by Hg2+ and Cu2+. The Kms of the enzyme for maltotetraose, maltopentaose, maltohexaose, maltoheptaose, and short chain amylose (DP 18) were 41.5 mM, 7.1 mM, 5.7 mM, 1.4 mM, and 0.6 mM, respectively. << Less

  Biosci Biotechnol Biochem 60:263-266(1996) [PubMed] [EuropePMC]