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Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius.
FEMS Microbiol Lett 2001; 194(2):201-6FM

Abstract

We report the molecular characterization and the detailed study of the recombinant maltooligosyl trehalose synthase mechanism from the thermoacidophilic archaeon Sulfolobus acidocaldarius. The mts gene encoding a maltooligosyl trehalose synthase was overexpressed in Escherichia coli using the T7-expression system. The purified recombinant enzyme exhibited optimum activity at 75 degrees C and pH 5 with citrate-phosphate buffer and retained 60% of residual activity after 72 h of incubation at 80 degrees C. The recombinant enzyme was active on maltooligosaccharides such as maltotriose, maltotetraose, maltopentaose and maltoheptaose. Investigation of the enzyme action on maltooligosaccharides has brought much insight into the reaction mechanism. Results obtained from thin-layer chromatography suggested a possible mechanism of action for maltooligosyl trehalose synthase: the enzyme, after converting the alpha-1,4-glucosidic linkage to an alpha-1,1-glucosidic linkage at the reducing end of maltooligosaccharide glc(n) is able to release glucose and maltooligosaccharide glc(n-1) residues. And then, the intramolecular transglycosylation and the hydrolytic reaction continue, with the maltooligosaccharide glc(n-1) until the initial maltooligosaccharide is reduced to maltose. An hypothetical mechanism of maltooligosyl trehalose synthase acting on maltooligosaccharide is proposed.

Authors+Show Affiliations

IFREMER Centre de Brest, DRV/VP Laboratoire de Biotechnologie des Micro-organismes Hydrothermaux, Plouzané, France. ygueguen@ifremer.frNo 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

11164309

Citation

Gueguen, Y, et al. "Characterization of the Maltooligosyl Trehalose Synthase From the Thermophilic Archaeon Sulfolobus Acidocaldarius." FEMS Microbiology Letters, vol. 194, no. 2, 2001, pp. 201-6.
Gueguen Y, Rolland JL, Schroeck S, et al. Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius. FEMS Microbiol Lett. 2001;194(2):201-6.
Gueguen, Y., Rolland, J. L., Schroeck, S., Flament, D., Defretin, S., Saniez, M. H., & Dietrich, J. (2001). Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius. FEMS Microbiology Letters, 194(2), pp. 201-6.
Gueguen Y, et al. Characterization of the Maltooligosyl Trehalose Synthase From the Thermophilic Archaeon Sulfolobus Acidocaldarius. FEMS Microbiol Lett. 2001 Jan 15;194(2):201-6. PubMed PMID: 11164309.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius. AU - Gueguen,Y, AU - Rolland,J L, AU - Schroeck,S, AU - Flament,D, AU - Defretin,S, AU - Saniez,M H, AU - Dietrich,J, PY - 2001/2/13/pubmed PY - 2001/6/2/medline PY - 2001/2/13/entrez SP - 201 EP - 6 JF - FEMS microbiology letters JO - FEMS Microbiol. Lett. VL - 194 IS - 2 N2 - We report the molecular characterization and the detailed study of the recombinant maltooligosyl trehalose synthase mechanism from the thermoacidophilic archaeon Sulfolobus acidocaldarius. The mts gene encoding a maltooligosyl trehalose synthase was overexpressed in Escherichia coli using the T7-expression system. The purified recombinant enzyme exhibited optimum activity at 75 degrees C and pH 5 with citrate-phosphate buffer and retained 60% of residual activity after 72 h of incubation at 80 degrees C. The recombinant enzyme was active on maltooligosaccharides such as maltotriose, maltotetraose, maltopentaose and maltoheptaose. Investigation of the enzyme action on maltooligosaccharides has brought much insight into the reaction mechanism. Results obtained from thin-layer chromatography suggested a possible mechanism of action for maltooligosyl trehalose synthase: the enzyme, after converting the alpha-1,4-glucosidic linkage to an alpha-1,1-glucosidic linkage at the reducing end of maltooligosaccharide glc(n) is able to release glucose and maltooligosaccharide glc(n-1) residues. And then, the intramolecular transglycosylation and the hydrolytic reaction continue, with the maltooligosaccharide glc(n-1) until the initial maltooligosaccharide is reduced to maltose. An hypothetical mechanism of maltooligosyl trehalose synthase acting on maltooligosaccharide is proposed. SN - 0378-1097 UR - https://www.unboundmedicine.com/medline/citation/11164309/Characterization_of_the_maltooligosyl_trehalose_synthase_from_the_thermophilic_archaeon_Sulfolobus_acidocaldarius_ L2 - https://academic.oup.com/femsle/article-lookup/doi/10.1111/j.1574-6968.2001.tb09470.x DB - PRIME DP - Unbound Medicine ER -