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A highly thermostable trehalase from the thermophilic bacterium Rhodothermus marinus.
Extremophiles 2007; 11(1):115-22E

Abstract

Trehalases play a central role in the metabolism of trehalose and can be found in a wide variety of organisms. A periplasmic trehalase (alpha,alpha-trehalose glucohydrolase, EC 3.2.1.28) from the thermophilic bacterium Rhodothermus marinus was purified and the respective encoding gene was identified, cloned and overexpressed in Escherichia coli. The recombinant trehalase is a monomeric protein with a molecular mass of 59 kDa. Maximum activity was observed at 88 degrees C and pH 6.5. The recombinant trehalase exhibited a K(m) of 0.16 mM and a V(max) of 81 micromol of trehalose (min)(-1) (mg of protein)(-1) at the optimal temperature for growth of R. marinus (65 degrees C) and pH 6.5. The enzyme was highly specific for trehalose and was inhibited by glucose with a K(i) of 7 mM. This is the most thermostable trehalase ever characterized. Moreover, this is the first report on the identification and characterization of a trehalase from a thermophilic bacterium.

Authors+Show Affiliations

Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apartado 127, 2780-156, Oeiras, Portugal.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16944251

Citation

Jorge, Carla D., et al. "A Highly Thermostable Trehalase From the Thermophilic Bacterium Rhodothermus Marinus." Extremophiles : Life Under Extreme Conditions, vol. 11, no. 1, 2007, pp. 115-22.
Jorge CD, Sampaio MM, Hreggvidsson GO, et al. A highly thermostable trehalase from the thermophilic bacterium Rhodothermus marinus. Extremophiles. 2007;11(1):115-22.
Jorge, C. D., Sampaio, M. M., Hreggvidsson, G. O., Kristjánson, J. K., & Santos, H. (2007). A highly thermostable trehalase from the thermophilic bacterium Rhodothermus marinus. Extremophiles : Life Under Extreme Conditions, 11(1), pp. 115-22.
Jorge CD, et al. A Highly Thermostable Trehalase From the Thermophilic Bacterium Rhodothermus Marinus. Extremophiles. 2007;11(1):115-22. PubMed PMID: 16944251.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A highly thermostable trehalase from the thermophilic bacterium Rhodothermus marinus. AU - Jorge,Carla D, AU - Sampaio,Maria Manuel, AU - Hreggvidsson,Gudmundur O, AU - Kristjánson,Jakob K, AU - Santos,Helena, Y1 - 2006/08/30/ PY - 2006/03/12/received PY - 2006/07/10/accepted PY - 2006/9/1/pubmed PY - 2007/7/12/medline PY - 2006/9/1/entrez SP - 115 EP - 22 JF - Extremophiles : life under extreme conditions JO - Extremophiles VL - 11 IS - 1 N2 - Trehalases play a central role in the metabolism of trehalose and can be found in a wide variety of organisms. A periplasmic trehalase (alpha,alpha-trehalose glucohydrolase, EC 3.2.1.28) from the thermophilic bacterium Rhodothermus marinus was purified and the respective encoding gene was identified, cloned and overexpressed in Escherichia coli. The recombinant trehalase is a monomeric protein with a molecular mass of 59 kDa. Maximum activity was observed at 88 degrees C and pH 6.5. The recombinant trehalase exhibited a K(m) of 0.16 mM and a V(max) of 81 micromol of trehalose (min)(-1) (mg of protein)(-1) at the optimal temperature for growth of R. marinus (65 degrees C) and pH 6.5. The enzyme was highly specific for trehalose and was inhibited by glucose with a K(i) of 7 mM. This is the most thermostable trehalase ever characterized. Moreover, this is the first report on the identification and characterization of a trehalase from a thermophilic bacterium. SN - 1431-0651 UR - https://www.unboundmedicine.com/medline/citation/16944251/A_highly_thermostable_trehalase_from_the_thermophilic_bacterium_Rhodothermus_marinus_ L2 - https://dx.doi.org/10.1007/s00792-006-0021-6 DB - PRIME DP - Unbound Medicine ER -