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Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius.
Biosci Biotechnol Biochem 1996; 60(2):263-6BB

Abstract

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.

Authors+Show Affiliations

Hayashibara Biochemical Laboratories, Inc., Okayama, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

9063973

Citation

Nakada, T, et al. "Purification and Characterization of Thermostable Maltooligosyl Trehalose Synthase From the Thermoacidophilic Archaebacterium Sulfolobus Acidocaldarius." Bioscience, Biotechnology, and Biochemistry, vol. 60, no. 2, 1996, pp. 263-6.
Nakada T, Ikegami S, Chaen H, et al. Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biosci Biotechnol Biochem. 1996;60(2):263-6.
Nakada, T., Ikegami, S., Chaen, H., Kubota, M., Fukuda, S., Sugimoto, T., ... Tsujisaka, Y. (1996). Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Bioscience, Biotechnology, and Biochemistry, 60(2), pp. 263-6.
Nakada T, et al. Purification and Characterization of Thermostable Maltooligosyl Trehalose Synthase From the Thermoacidophilic Archaebacterium Sulfolobus Acidocaldarius. Biosci Biotechnol Biochem. 1996;60(2):263-6. PubMed PMID: 9063973.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. AU - Nakada,T, AU - Ikegami,S, AU - Chaen,H, AU - Kubota,M, AU - Fukuda,S, AU - Sugimoto,T, AU - Kurimoto,M, AU - Tsujisaka,Y, PY - 1996/2/1/pubmed PY - 1996/2/1/medline PY - 1996/2/1/entrez SP - 263 EP - 6 JF - Bioscience, biotechnology, and biochemistry JO - Biosci. Biotechnol. Biochem. VL - 60 IS - 2 N2 - 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. SN - 0916-8451 UR - https://www.unboundmedicine.com/medline/citation/9063973/Purification_and_characterization_of_thermostable_maltooligosyl_trehalose_synthase_from_the_thermoacidophilic_archaebacterium_Sulfolobus_acidocaldarius_ L2 - http://joi.jlc.jst.go.jp/JST.Journalarchive/bbb1992/60.263?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -