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Characterization of a trehalose-degrading enzyme from the hyperthermophilic archaeon Sulfolobus acidocaldarius.
J Biosci Bioeng 2016; 122(1):47-51JB

Abstract

We purified a cytosolic trehalase (TreH) from a thermoacidophilic archaeon Sulfolobus acidocaldarius. Enzyme activity in cell-free extracts indicated that trehalose degradation in the cell occurred via the hydrolytic activity of TreH, and not via TreP (phosphorolytic activity) or TreT (transfer activity). TreH was purified to near-homogeneity by DEAE anion-exchange chromatography, followed by size exclusion and HiTrap Q anion-exchange chromatography, and its molecular mass was estimated as 40 kDa. Maximum activity was observed at 85°C and pH 4.5. The half-life of TreH was 53 and 41 min at 90°C and 95°C, respectively. TreH was highly specific for trehalose and was inhibited by glucose with a Ki of 0.05 mM. Compared with TreH from other trehalases, TreH from S. acidocaldarius is the most thermostable trehalase reported so far. Furthermore, this is the first trehalase characterized in the Archaea domain.

Authors+Show Affiliations

Department of Microbiology, College of Natural Sciences, Pusan National University, 2, Busandaehak-ro 63beon-gil, Geumjeong-gu, Busan 46241, Republic of Korea.Department of Microbiology, College of Natural Sciences, Pusan National University, 2, Busandaehak-ro 63beon-gil, Geumjeong-gu, Busan 46241, Republic of Korea.Department of Microbiology, College of Natural Sciences, Pusan National University, 2, Busandaehak-ro 63beon-gil, Geumjeong-gu, Busan 46241, Republic of Korea.Department of Microbiology, College of Natural Sciences, Pusan National University, 2, Busandaehak-ro 63beon-gil, Geumjeong-gu, Busan 46241, Republic of Korea.Department of Microbiology, College of Natural Sciences, Pusan National University, 2, Busandaehak-ro 63beon-gil, Geumjeong-gu, Busan 46241, Republic of Korea. Electronic address: jhcha@pusan.ac.kr.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

26811220

Citation

Moon, Jeong Hyun, et al. "Characterization of a Trehalose-degrading Enzyme From the Hyperthermophilic Archaeon Sulfolobus Acidocaldarius." Journal of Bioscience and Bioengineering, vol. 122, no. 1, 2016, pp. 47-51.
Moon JH, Lee W, Park J, et al. Characterization of a trehalose-degrading enzyme from the hyperthermophilic archaeon Sulfolobus acidocaldarius. J Biosci Bioeng. 2016;122(1):47-51.
Moon, J. H., Lee, W., Park, J., Choi, K. H., & Cha, J. (2016). Characterization of a trehalose-degrading enzyme from the hyperthermophilic archaeon Sulfolobus acidocaldarius. Journal of Bioscience and Bioengineering, 122(1), pp. 47-51. doi:10.1016/j.jbiosc.2015.12.011.
Moon JH, et al. Characterization of a Trehalose-degrading Enzyme From the Hyperthermophilic Archaeon Sulfolobus Acidocaldarius. J Biosci Bioeng. 2016;122(1):47-51. PubMed PMID: 26811220.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of a trehalose-degrading enzyme from the hyperthermophilic archaeon Sulfolobus acidocaldarius. AU - Moon,Jeong Hyun, AU - Lee,Whiso, AU - Park,Jihee, AU - Choi,Kyoung-Hwa, AU - Cha,Jaeho, Y1 - 2016/01/19/ PY - 2015/10/24/received PY - 2015/12/15/revised PY - 2015/12/15/accepted PY - 2016/1/27/entrez PY - 2016/1/27/pubmed PY - 2017/3/10/medline KW - Substrate specificity KW - Sulfolobus acidocaldarius KW - Trehalase KW - Trehalose SP - 47 EP - 51 JF - Journal of bioscience and bioengineering JO - J. Biosci. Bioeng. VL - 122 IS - 1 N2 - We purified a cytosolic trehalase (TreH) from a thermoacidophilic archaeon Sulfolobus acidocaldarius. Enzyme activity in cell-free extracts indicated that trehalose degradation in the cell occurred via the hydrolytic activity of TreH, and not via TreP (phosphorolytic activity) or TreT (transfer activity). TreH was purified to near-homogeneity by DEAE anion-exchange chromatography, followed by size exclusion and HiTrap Q anion-exchange chromatography, and its molecular mass was estimated as 40 kDa. Maximum activity was observed at 85°C and pH 4.5. The half-life of TreH was 53 and 41 min at 90°C and 95°C, respectively. TreH was highly specific for trehalose and was inhibited by glucose with a Ki of 0.05 mM. Compared with TreH from other trehalases, TreH from S. acidocaldarius is the most thermostable trehalase reported so far. Furthermore, this is the first trehalase characterized in the Archaea domain. SN - 1347-4421 UR - https://www.unboundmedicine.com/medline/citation/26811220/Characterization_of_a_trehalose_degrading_enzyme_from_the_hyperthermophilic_archaeon_Sulfolobus_acidocaldarius_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1389-1723(15)00448-X DB - PRIME DP - Unbound Medicine ER -